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Conserved domains on  [gi|1418826391|gb|RAZ83892|]
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photosynthetic reaction center subunit H [Cereibacter johrii]

Protein Classification

photosynthetic reaction center subunit H( domain architecture ID 11490218)

photosystem reaction center subunit H (PRCH) is a component of the reaction center (RC), which is an integral membrane protein-pigment complex that catalyzes light-induced reduction of ubiquinone to ubiquinol, generating a transmembrane electrochemical gradient of protons used to produce ATP by ATP synthase

CATH:  4.10.540.10|3.90.50.10
Gene Ontology:  GO:0019684|GO:0042314
PubMed:  12429060
SCOP:  4001979|4002050
TCDB:  3.E.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
puhA TIGR01150
photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic ...
 1-248 6.08e-156

photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic reaction center H subunit in non-oxygenic photosynthetic bacteria. The reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reaction center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in the form of NADH. Ultimately, the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is an organic acid rather than water. Much of our current functional understanding of photosynthesis comes from the structural determination and spectroscopic studies on the reaction center of Rhodobacter sphaeroides. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]


:

Pssm-ID: 273470  Cd Length: 252  Bit Score: 433.51  E-value: 6.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   1 MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDG--TPAANQG-PFPLPKPKTFILPHGRgTLTVPG 77
Cdd:TIGR01150   1 MVGGALFGHFDLAQLVIYAFWIFLAGLIYYLRREDRREGYPLENPDGlvKLAPNQGqVFPLPYPKTFVLPHGR-TVTVPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391  78 PESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSAG-KNPIGLPVRGC 156
Cdd:TIGR01150  80 REPETREIKLARTAVFEGAPFQPTGNPMVDAVGPASYAERRELPDLTVHGHNKIVPLRVATDFSVAAGdVDPRGLPVVAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391 157 DLEIAGKVVDIWVDIPEQMARFLEVELKDG-STRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICG 235
Cdd:TIGR01150 160 DGEVAGKVTDLWVDRPEQYFRYLEVELAGGaRTALLPMGMCKVKSDRVVVNSILSDLFANVPTIKSPDQITLREEDKVSA 239

                         250
                  ....*....|...
gi 1418826391 236 YVAGGLMYAAPKR 248
Cdd:TIGR01150 240 YYAGGLLYATPER 252
 
Name Accession Description Interval E-value
puhA TIGR01150
photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic ...
 1-248 6.08e-156

photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic reaction center H subunit in non-oxygenic photosynthetic bacteria. The reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reaction center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in the form of NADH. Ultimately, the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is an organic acid rather than water. Much of our current functional understanding of photosynthesis comes from the structural determination and spectroscopic studies on the reaction center of Rhodobacter sphaeroides. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]


Pssm-ID: 273470  Cd Length: 252  Bit Score: 433.51  E-value: 6.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   1 MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDG--TPAANQG-PFPLPKPKTFILPHGRgTLTVPG 77
Cdd:TIGR01150   1 MVGGALFGHFDLAQLVIYAFWIFLAGLIYYLRREDRREGYPLENPDGlvKLAPNQGqVFPLPYPKTFVLPHGR-TVTVPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391  78 PESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSAG-KNPIGLPVRGC 156
Cdd:TIGR01150  80 REPETREIKLARTAVFEGAPFQPTGNPMVDAVGPASYAERRELPDLTVHGHNKIVPLRVATDFSVAAGdVDPRGLPVVAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391 157 DLEIAGKVVDIWVDIPEQMARFLEVELKDG-STRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICG 235
Cdd:TIGR01150 160 DGEVAGKVTDLWVDRPEQYFRYLEVELAGGaRTALLPMGMCKVKSDRVVVNSILSDLFANVPTIKSPDQITLREEDKVSA 239

                         250
                  ....*....|...
gi 1418826391 236 YVAGGLMYAAPKR 248
Cdd:TIGR01150 240 YYAGGLLYATPER 252
PRCH cd00226
Photosynthetic reaction center (RC) complex, subunit H; RC is an integral membrane ...
 1-245 1.56e-152

Photosynthetic reaction center (RC) complex, subunit H; RC is an integral membrane protein-pigment complex which catalyzes light-induced reduction of ubiquinone to ubiquinol, generating a transmembrane electrochemical gradient of protons used to produce ATP by ATP synthase. Subunit H is positioned mainly in the cytoplasm with one transmembrane alpha helix. Provides proton transfer pathway (water channels) connecting the terminal quinone electron acceptor of RC, to the aqueous phase. Found in photosynthetic bacteria: alpha, beta, and gamma proteobacteria.


Pssm-ID: 238138  Cd Length: 246  Bit Score: 424.93  E-value: 1.56e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   1 MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGrGTLTVPGPES 80
Cdd:cd00226     1 MVGGAIFQYFDLAQLVIYAFWIFFAGLIYYLRRENMREGYPLEDPDGGPSENGGVFPLPYPKTFKLPHG-GTVTVPRVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391  81 EDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSA-GKNPIGLPVRGCDLE 159
Cdd:cd00226    80 ETRALALARTAPFEGAPLVPTGNPMLDGVGPASWAERRDLPDLDVHGHPKIVPMRVATGFSVAAgDVDPRGLPVVGADGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391 160 IAGKVVDIWVDIPEQMARFLEVELKD-GSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVA 238
Cdd:cd00226   160 VAGKVTDLWVDRPEQLFRYLEVELAGgGRTVLLPMGFAKVKSDRVKVTAILSEHFANVPTIKSPDQVTLLEEDKICAYYA 239


                  ....*..
gi 1418826391 239 GGLMYAA 245
Cdd:cd00226   240 GGLLYAT 246
PRCH pfam03967
Photosynthetic reaction centre, H-chain N-terminal region; The family corresponds the ...
 7-136 7.83e-79

Photosynthetic reaction centre, H-chain N-terminal region; The family corresponds the N-terminal cytoplasmic domain.


Pssm-ID: 397870  Cd Length: 133  Bit Score: 234.05  E-value: 7.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   7 FGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGRGTLTVPGPESEDRPIA 86
Cdd:pfam03967   4 TGYIDVAQLVLYAFWIFFAGLIFYLRREDKREGYPLESDDGGRAKNQGFPPVPSPKTFKLPHGGGTVTVPRPENEQTDLA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418826391  87 LARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKA 136
Cdd:pfam03967  84 ATPTAPWPGAPLEPTGNPMLDGVGPGSWAQRADVPDLTLEGHPRIVPLRV 133
 
Name Accession Description Interval E-value
puhA TIGR01150
photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic ...
 1-248 6.08e-156

photosynthetic reaction center, subunit H, bacterial; This model describes the photosynthetic reaction center H subunit in non-oxygenic photosynthetic bacteria. The reaction center is an integral membrane pigment-protein that carries out light-driven electron transfer reactions. At the core of reaction center is a collection light-harvesting cofactors and closely associated polypeptides. The core protein complex is made of L, M and H subunits. The common cofactors include bacterichlorophyll, bacteriopheophytins, ubiquinone and no-heme ferrous iron. The net result of electron tranfer reactions is the establishment of proton electrochemical gradient and production of reducing equivalents in the form of NADH. Ultimately, the process results in the reduction of C02 to carbohydrates(C6H12O6) In non-oxygenic organisms, the electron donor is an organic acid rather than water. Much of our current functional understanding of photosynthesis comes from the structural determination and spectroscopic studies on the reaction center of Rhodobacter sphaeroides. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]


Pssm-ID: 273470  Cd Length: 252  Bit Score: 433.51  E-value: 6.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   1 MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDG--TPAANQG-PFPLPKPKTFILPHGRgTLTVPG 77
Cdd:TIGR01150   1 MVGGALFGHFDLAQLVIYAFWIFLAGLIYYLRREDRREGYPLENPDGlvKLAPNQGqVFPLPYPKTFVLPHGR-TVTVPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391  78 PESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSAG-KNPIGLPVRGC 156
Cdd:TIGR01150  80 REPETREIKLARTAVFEGAPFQPTGNPMVDAVGPASYAERRELPDLTVHGHNKIVPLRVATDFSVAAGdVDPRGLPVVAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391 157 DLEIAGKVVDIWVDIPEQMARFLEVELKDG-STRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICG 235
Cdd:TIGR01150 160 DGEVAGKVTDLWVDRPEQYFRYLEVELAGGaRTALLPMGMCKVKSDRVVVNSILSDLFANVPTIKSPDQITLREEDKVSA 239

                         250
                  ....*....|...
gi 1418826391 236 YVAGGLMYAAPKR 248
Cdd:TIGR01150 240 YYAGGLLYATPER 252
PRCH cd00226
Photosynthetic reaction center (RC) complex, subunit H; RC is an integral membrane ...
 1-245 1.56e-152

Photosynthetic reaction center (RC) complex, subunit H; RC is an integral membrane protein-pigment complex which catalyzes light-induced reduction of ubiquinone to ubiquinol, generating a transmembrane electrochemical gradient of protons used to produce ATP by ATP synthase. Subunit H is positioned mainly in the cytoplasm with one transmembrane alpha helix. Provides proton transfer pathway (water channels) connecting the terminal quinone electron acceptor of RC, to the aqueous phase. Found in photosynthetic bacteria: alpha, beta, and gamma proteobacteria.


Pssm-ID: 238138  Cd Length: 246  Bit Score: 424.93  E-value: 1.56e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   1 MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGrGTLTVPGPES 80
Cdd:cd00226     1 MVGGAIFQYFDLAQLVIYAFWIFFAGLIYYLRRENMREGYPLEDPDGGPSENGGVFPLPYPKTFKLPHG-GTVTVPRVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391  81 EDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSA-GKNPIGLPVRGCDLE 159
Cdd:cd00226    80 ETRALALARTAPFEGAPLVPTGNPMLDGVGPASWAERRDLPDLDVHGHPKIVPMRVATGFSVAAgDVDPRGLPVVGADGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391 160 IAGKVVDIWVDIPEQMARFLEVELKD-GSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVA 238
Cdd:cd00226   160 VAGKVTDLWVDRPEQLFRYLEVELAGgGRTVLLPMGFAKVKSDRVKVTAILSEHFANVPTIKSPDQVTLLEEDKICAYYA 239


                  ....*..
gi 1418826391 239 GGLMYAA 245
Cdd:cd00226   240 GGLLYAT 246
PRCH pfam03967
Photosynthetic reaction centre, H-chain N-terminal region; The family corresponds the ...
 7-136 7.83e-79

Photosynthetic reaction centre, H-chain N-terminal region; The family corresponds the N-terminal cytoplasmic domain.


Pssm-ID: 397870  Cd Length: 133  Bit Score: 234.05  E-value: 7.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418826391   7 FGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGRGTLTVPGPESEDRPIA 86
Cdd:pfam03967   4 TGYIDVAQLVLYAFWIFFAGLIFYLRREDKREGYPLESDDGGRAKNQGFPPVPSPKTFKLPHGGGTVTVPRPENEQTDLA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418826391  87 LARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKA 136
Cdd:pfam03967  84 ATPTAPWPGAPLEPTGNPMLDGVGPGSWAQRADVPDLTLEGHPRIVPLRV 133
PRC pfam05239
PRC-barrel domain; The PRC-barrel is an all beta barrel domain found in photosystem reaction ...
 140-212 8.45e-10

PRC-barrel domain; The PRC-barrel is an all beta barrel domain found in photosystem reaction centre subunit H of the purple bacteria and RNA metabolism proteins of the RimM group. PRC-barrels are approximately 80 residues long, and found widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain.


Pssm-ID: 398765  Cd Length: 78  Bit Score: 53.83  E-value: 8.45e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418826391 140 FHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGS---TRLLPM--QMVKVQSNRVHVNALSSDL 212
Cdd:pfam05239   1 EDEFYASDLIGLEVYTEDGEKLGKVKDVVIDEGEGRVRYLVVSVGGFLggkEVLIPFdkLNVKLGKDRIIVDPPKELL 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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