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Conserved domains on  [gi|15596749|ref|NP_250243|]
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cytochrome C oxidase cbb3-type subunit CcoP [Pseudomonas aeruginosa PAO1]

Protein Classification

cytochrome c family protein( domain architecture ID 229496)

cytochrome c family protein is a ubiquitous heme protein in mitochondria and bacteria, possessing a CXXCH motif with covalently attached heme; in both prokaryotes and eukaryotes it functions to transfer electrons from reduced substrates to physiological partners, thereby driving the pathway leading to oxidative phosphorylation and ATP synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHOR super family cl21467
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It ...
29-314 4.73e-92

Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It carries the two characteriztic Cys-X-Y-Cys-His haem-binding motifs. The C-terminal high-potential site functions as an electron transfer centre, and the N-terminal low-potential site corresponds to the peroxidatic centre. Its probable function is as a peroxidase.


The actual alignment was detected with superfamily member TIGR00782:

Pssm-ID: 473872 [Multi-domain]  Cd Length: 285  Bit Score: 275.24  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749    29 KGQRSSTTDETVGHSYDGIEEYDNPLPKWWFMLFVGTLVFAVGYLALYPGLGTWKGLMPGYQsadefadkekGWTGVHQW 108
Cdd:TIGR00782   1 KDPKSQGEVQTTGHEWDGIEEYDNPLPRWWLWTFYATIVWGFGYLVAYPAWPLVSGATKGLL----------GWSSRSQV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   109 EKEMAKADEKYGPIFAKFAAMPIEEVAKDPQAVKM----GGRLFASNCSICHGSDAKGAYGFPNLTDADWRWGGEPETIK 184
Cdd:TIGR00782  71 EEEIKKFNEKNAAKWAKLAQTPLEDIAKDPELKQYarnaGAAIFRTWCAQCHGSGAGGAKGFPNLLDNDWLWGGTLEGIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   185 TTIMAGRH---------AAMPAWGEVIGEEGVKNVAAFVLtqmdgrKLPEGAKAD---IEAGKQVFATTCVACHGPEGKG 252
Cdd:TIGR00782 151 TTIKHGIRdpddgdtyvGEMPAFGPLLEEADIKDVASYVM------SLSSGKPKDealAAKGQELFADNCTTCHGEDGKG 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596749   253 TPAMGAPDLTHpGAFIYGSSFAQLQQTIRYGRQGVMPAQQEHLGNDKVHLLAAYVYSLSHGE 314
Cdd:TIGR00782 225 LQELGAPNLTD-DVWLYGGDLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYVHSLGGGQ 285
 
Name Accession Description Interval E-value
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
29-314 4.73e-92

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: 275.24  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749    29 KGQRSSTTDETVGHSYDGIEEYDNPLPKWWFMLFVGTLVFAVGYLALYPGLGTWKGLMPGYQsadefadkekGWTGVHQW 108
Cdd:TIGR00782   1 KDPKSQGEVQTTGHEWDGIEEYDNPLPRWWLWTFYATIVWGFGYLVAYPAWPLVSGATKGLL----------GWSSRSQV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   109 EKEMAKADEKYGPIFAKFAAMPIEEVAKDPQAVKM----GGRLFASNCSICHGSDAKGAYGFPNLTDADWRWGGEPETIK 184
Cdd:TIGR00782  71 EEEIKKFNEKNAAKWAKLAQTPLEDIAKDPELKQYarnaGAAIFRTWCAQCHGSGAGGAKGFPNLLDNDWLWGGTLEGIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   185 TTIMAGRH---------AAMPAWGEVIGEEGVKNVAAFVLtqmdgrKLPEGAKAD---IEAGKQVFATTCVACHGPEGKG 252
Cdd:TIGR00782 151 TTIKHGIRdpddgdtyvGEMPAFGPLLEEADIKDVASYVM------SLSSGKPKDealAAKGQELFADNCTTCHGEDGKG 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596749   253 TPAMGAPDLTHpGAFIYGSSFAQLQQTIRYGRQGVMPAQQEHLGNDKVHLLAAYVYSLSHGE 314
Cdd:TIGR00782 225 LQELGAPNLTD-DVWLYGGDLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYVHSLGGGQ 285
FixP_N pfam14715
N-terminal domain of cytochrome oxidase-cbb3, FixP; This is the N-terminal domain of FixP, the ...
37-83 1.62e-22

N-terminal domain of cytochrome oxidase-cbb3, FixP; This is the N-terminal domain of FixP, the cytochrome oxidase type-cbb3. the exact function is not known.


Pssm-ID: 464278  Cd Length: 48  Bit Score: 88.37  E-value: 1.62e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15596749    37 DETVGHSYDGIEEYDNPLPKWWFMLFVGTLVFAVGYLALYPGLGTWK 83
Cdd:pfam14715   2 DETTGHEWDGIRELNNPLPRWWLWLFYATIVFAVVYLVLYPGLGLGQ 48
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
55-217 1.54e-20

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 86.93  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749  55 PKWWFMLFVGTLVFAVGYLALYPGLGTWKGLMPGYQSADEFADKEKGWTGVHQWEKEMAKADEKYGPIFAKFAAMPIEEV 134
Cdd:COG2010   3 LLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAADAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 135 AKDPQAVKMGGRLFASNCSICHGSDAKGAYG-FPNLTDADwRWGGEPETIKTTIMAGR-HAAMPAWGEVIGEEGVKNVAA 212
Cdd:COG2010  83 AADAEALARGKALYEQNCAACHGADGKGGLGaAPNLTDDA-LYGGDPEALVETILNGRpGGAMPAFGGQLSDEEIAALAA 161

                ....*
gi 15596749 213 FVLTQ 217
Cdd:COG2010 162 YLRSL 166
PRK13697 PRK13697
cytochrome c6; Provisional
144-219 5.97e-05

cytochrome c6; Provisional


Pssm-ID: 184253 [Multi-domain]  Cd Length: 111  Bit Score: 41.69  E-value: 5.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596749  144 GGRLFASNCSICHGSDAKGAYGFPNLTDADWRWGG--EPETIKTTIMAGRHAaMPAWGEVIGEEGVKNVAAFVLTQMD 219
Cdd:PRK13697  31 GEQVFSANCASCHAGGKNLVNAGKTLKKADLEKYGmySLEAITAQVTNGKNA-MPAFKDRLSPDQIEDVAAYVLEQAE 107
 
Name Accession Description Interval E-value
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
29-314 4.73e-92

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: 275.24  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749    29 KGQRSSTTDETVGHSYDGIEEYDNPLPKWWFMLFVGTLVFAVGYLALYPGLGTWKGLMPGYQsadefadkekGWTGVHQW 108
Cdd:TIGR00782   1 KDPKSQGEVQTTGHEWDGIEEYDNPLPRWWLWTFYATIVWGFGYLVAYPAWPLVSGATKGLL----------GWSSRSQV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   109 EKEMAKADEKYGPIFAKFAAMPIEEVAKDPQAVKM----GGRLFASNCSICHGSDAKGAYGFPNLTDADWRWGGEPETIK 184
Cdd:TIGR00782  71 EEEIKKFNEKNAAKWAKLAQTPLEDIAKDPELKQYarnaGAAIFRTWCAQCHGSGAGGAKGFPNLLDNDWLWGGTLEGIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   185 TTIMAGRH---------AAMPAWGEVIGEEGVKNVAAFVLtqmdgrKLPEGAKAD---IEAGKQVFATTCVACHGPEGKG 252
Cdd:TIGR00782 151 TTIKHGIRdpddgdtyvGEMPAFGPLLEEADIKDVASYVM------SLSSGKPKDealAAKGQELFADNCTTCHGEDGKG 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596749   253 TPAMGAPDLTHpGAFIYGSSFAQLQQTIRYGRQGVMPAQQEHLGNDKVHLLAAYVYSLSHGE 314
Cdd:TIGR00782 225 LQELGAPNLTD-DVWLYGGDLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYVHSLGGGQ 285
FixP_N pfam14715
N-terminal domain of cytochrome oxidase-cbb3, FixP; This is the N-terminal domain of FixP, the ...
37-83 1.62e-22

N-terminal domain of cytochrome oxidase-cbb3, FixP; This is the N-terminal domain of FixP, the cytochrome oxidase type-cbb3. the exact function is not known.


Pssm-ID: 464278  Cd Length: 48  Bit Score: 88.37  E-value: 1.62e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15596749    37 DETVGHSYDGIEEYDNPLPKWWFMLFVGTLVFAVGYLALYPGLGTWK 83
Cdd:pfam14715   2 DETTGHEWDGIRELNNPLPRWWLWLFYATIVFAVVYLVLYPGLGLGQ 48
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
55-217 1.54e-20

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 86.93  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749  55 PKWWFMLFVGTLVFAVGYLALYPGLGTWKGLMPGYQSADEFADKEKGWTGVHQWEKEMAKADEKYGPIFAKFAAMPIEEV 134
Cdd:COG2010   3 LLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAADAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 135 AKDPQAVKMGGRLFASNCSICHGSDAKGAYG-FPNLTDADwRWGGEPETIKTTIMAGR-HAAMPAWGEVIGEEGVKNVAA 212
Cdd:COG2010  83 AADAEALARGKALYEQNCAACHGADGKGGLGaAPNLTDDA-LYGGDPEALVETILNGRpGGAMPAFGGQLSDEEIAALAA 161

                ....*
gi 15596749 213 FVLTQ 217
Cdd:COG2010 162 YLRSL 166
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
162-313 1.90e-17

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 78.45  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 162 GAYGFPNLTDADWRWGGEPETIKTTIMAGRHAAMPAWGEVIGEEGVKNVAAFVLTQMDGRKLPEGAKADIEAGKQVFATT 241
Cdd:COG2010  20 EGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAADAPAADAEALARGKALYEQN 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596749 242 CVACHGPEGKGTPAMgAPDLThpGAFIYGSSFAQLQQTIRYGR-QGVMPAQQEHLGNDKVHLLAAYVYSLSHG 313
Cdd:COG2010 100 CAACHGADGKGGLGA-APNLT--DDALYGGDPEALVETILNGRpGGAMPAFGGQLSDEEIAALAAYLRSLSGN 169
TsdA COG3258
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ...
140-312 4.17e-16

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


Pssm-ID: 442489 [Multi-domain]  Cd Length: 216  Bit Score: 75.66  E-value: 4.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 140 AVKMGGRLFAS--NCSICHGSDAKGAYGFPNLTDADWRWGGEPETIKTTIMAGRHAAMPAWGEVIGEEGVKNVAAFVLTQ 217
Cdd:COG3258  11 AARRGEELFTNglSCASCHLDAGTKPWGVAAAYPAYRARNGKVVTLEDRINGCFTRSMNGKPLPLDSAEMKALVAYLRWL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 218 ---------MDGRKLPE----GAKADIEAGKQVFATTCVACHGPEGKGTPAMGA----PDLTHPGAFIYGSSFAQLQQTI 280
Cdd:COG3258  91 srglpvgvkLDGRGLPKlpkpAASADVERGKALYAERCASCHGADGEGQGRADGqygfPPLWGGDSYNDGAGMARLGTLA 170
                       170       180       190
                ....*....|....*....|....*....|...
gi 15596749 281 RYGRQGVMPA-QQEHLGNDKVHLLAAYVYSLSH 312
Cdd:COG3258 171 DFIKGRNMPLgKPGSLSDDEAWDVAAYVRSLPR 203
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
227-317 7.96e-15

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 68.99  E-value: 7.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 227 AKADIEAGKQvFATTCVACHGPEGKGTPAMGAPDLT--HPGAFIygssfAQLQQtIRYGRQ--GVMPAQQEHLGNDKVHL 302
Cdd:COG2863  11 AAGDAARGKA-YAAACAACHGADGEGNPGGGAPRLAgqHAEYLV-----AQLKA-FRSGARknGVMPAIAKGLSDEDIKA 83
                        90
                ....*....|....*
gi 15596749 303 LAAYVYSLSHGEKSA 317
Cdd:COG2863  84 LAAYIASLKAPPGAA 98
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
139-214 2.50e-12

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 61.27  E-value: 2.50e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596749   139 QAVKMGGRLFASNCSICHGSDAKGaygfPNLTDADWrwggEPETIKTTIMAGRhAAMPAWGEVIGEEGVKNVAAFV 214
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAG----PSLAGRAL----PPEALVDIIRNGK-GAMPAFGGDLSDEELEALAAYL 67
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
229-307 2.21e-08

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 50.10  E-value: 2.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596749   229 ADIEAGKQVFATTCVACHGPEGKGtPAMGAPDLTHpgafiygssfAQLQQTIRYGRqGVMPAQQEHLGNDKVHLLAAYV 307
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAG-PSLAGRALPP----------EALVDIIRNGK-GAMPAFGGDLSDEELEALAAYL 67
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
125-217 1.08e-07

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 48.96  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749 125 KFAAMPIEEVAKDPQAvkmgGRLFASNCSICHGSDAKG--AYGFPNLTDADwrwggePETIKTTIMAGR-----HAAMPA 197
Cdd:COG2863   2 KLALLAAPAAAGDAAR----GKAYAAACAACHGADGEGnpGGGAPRLAGQH------AEYLVAQLKAFRsgarkNGVMPA 71
                        90       100
                ....*....|....*....|
gi 15596749 198 WGEVIGEEGVKNVAAFVLTQ 217
Cdd:COG2863  72 IAKGLSDEDIKALAAYIASL 91
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
232-311 2.40e-07

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: 47.92  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   232 EAGKQVFATTCVACHGPEGKGTPAMGaPDLTHPGA-----------FIYGSSFAQLQQTIRYGRQGVMPAQQEhLGNDKV 300
Cdd:pfam00034   1 ARGKKLFAANCAACHGVNGEGAGAGG-PDLAGLAArypgdalgairENKHAIGGGGVDRAGGPPGTGMPAFDG-LTDEEI 78
                          90
                  ....*....|.
gi 15596749   301 HLLAAYVYSLS 311
Cdd:pfam00034  79 ADLVAYLLSLS 89
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
144-216 5.74e-07

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: 46.76  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   144 GGRLFASNCSICHGSDAKGAY-GFPNLTDADWRWGGEPE------------TIKTTIMAGRHAAMPAWGEvIGEEGVKNV 210
Cdd:pfam00034   3 GKKLFAANCAACHGVNGEGAGaGGPDLAGLAARYPGDALgairenkhaiggGGVDRAGGPPGTGMPAFDG-LTDEEIADL 81

                  ....*.
gi 15596749   211 AAFVLT 216
Cdd:pfam00034  82 VAYLLS 87
PRK13697 PRK13697
cytochrome c6; Provisional
144-219 5.97e-05

cytochrome c6; Provisional


Pssm-ID: 184253 [Multi-domain]  Cd Length: 111  Bit Score: 41.69  E-value: 5.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596749  144 GGRLFASNCSICHGSDAKGAYGFPNLTDADWRWGG--EPETIKTTIMAGRHAaMPAWGEVIGEEGVKNVAAFVLTQMD 219
Cdd:PRK13697  31 GEQVFSANCASCHAGGKNLVNAGKTLKKADLEKYGmySLEAITAQVTNGKNA-MPAFKDRLSPDQIEDVAAYVLEQAE 107
petJ CHL00183
cytochrome c553; Provisional
144-219 1.13e-04

cytochrome c553; Provisional


Pssm-ID: 177085  Cd Length: 108  Bit Score: 40.91  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749  144 GGRLFASNCSICH-------------GSDAKGAYGFPNLtdadwrwggepETIKTTIMAGRHAaMPAWGEVIGEEGVKNV 210
Cdd:CHL00183  29 GEQIFSANCAACHaggnnvimpektlKKDALEANSMNSI-----------EAITYQVTNGKNA-MPAFGGRLSDEDIEDV 96

                 ....*....
gi 15596749  211 AAFVLTQMD 219
Cdd:CHL00183  97 ANYVLSQAE 105
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
229-263 1.47e-04

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 40.25  E-value: 1.47e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15596749 229 ADIEAGKQVFATTCVACHGPEGKGTPAMGaPDLTH 263
Cdd:COG3474   1 GDAAAGEKLFNRKCAACHSVDGGAGNRVG-PNLNG 34
CxxCH_TIGR02603 TIGR02603
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ...
229-262 1.69e-04

putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).


Pssm-ID: 274224  Cd Length: 133  Bit Score: 40.81  E-value: 1.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 15596749   229 ADIEAGKQVFATTCVACHGPEGKGTPAmgAPDLT 262
Cdd:TIGR02603   1 GDAARGKAVFAKVCYLCHRIGGQGVDF--GPNLT 32
PRK14486 PRK14486
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
134-217 2.50e-04

putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional


Pssm-ID: 184704 [Multi-domain]  Cd Length: 294  Bit Score: 42.11  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749  134 VAKDPQAVKMGGRLFASNCSICHGSDAKGAYGfPNLTDADwrWGGEPET-IKTTIMAGRHA-AMPAWGEVIGEEGVKNVA 211
Cdd:PRK14486 208 FATDVAAIAKGKALYDANCAACHGDEAQGQEG-VALNDID--DGDLPDAaYFGMIKGGSDAkGMPGFGGDLSDDDIWAIV 284

                 ....*.
gi 15596749  212 AFVLTQ 217
Cdd:PRK14486 285 AYIRSQ 290
thiosulf_SoxX TIGR04485
sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome ...
242-310 7.66e-03

sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxA. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate.


Pssm-ID: 275278 [Multi-domain]  Cd Length: 78  Bit Score: 34.87  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596749   242 CVACHGPEGKGT-PAMGAPDLTHpgafiYGSSF---AQLQQTI-------------RYGRQGVMPAQQehlgndkVHLLA 304
Cdd:TIGR04485   5 CLACHQIPGSEVfPGNIGPSLTG-----YGARYpdeAYLRAKIadakavnpctvmpRFGKNGILTEQE-------IEDVV 72

                  ....*.
gi 15596749   305 AYVYSL 310
Cdd:TIGR04485  73 AYLLTL 78
 
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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