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Conserved domains on  [gi|1569087971|gb|RYJ09576|]
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halocyanin domain-containing protein [Haloarcula hispanica]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10798999)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 169-282 1.59e-64

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


:

Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 201.93  E-value: 1.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 169 YGGWFDDVSNYDGTTVDRTDADSVEISVGAQGNNGAFAFDPPAVRVTPGTEVTWKWTGEGGGHNVVSDGDGPLDSGGAVS 248
Cdd:TIGR03102   1 YDGFLDDVSNYDGSIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1569087971 249 EAGTTYSHTFEEMGVYKYVCVPHESLGMKGAVVV 282
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVV 114
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 32-145 8.45e-62

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


:

Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 195.00  E-value: 8.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  32 YGGWFDDVSNYDG-TADKRGQDTVTITVGAQGNNGAFAFDPPAVMVSPGTEVVWEWNGEGGGHNVVSDGDGPLDSGGAVS 110
Cdd:TIGR03102   1 YDGFLDDVSNYDGsIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1569087971 111 EAGTTYSHTFESEGMFKYVCVPHEALGMKGAVVVR 145
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVVE 115
SPC25 super family cl05974
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
 379-401 3.78e-03

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


The actual alignment was detected with superfamily member pfam06703:

Pssm-ID: 461993  Cd Length: 153  Bit Score: 37.56  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|...
gi 1569087971 379 TAALVAFYFVLIALLWVFMYFVE 401
Cdd:pfam06703  54 LIVCVALYFILSGILTLWTKFVE 76
 
Name Accession Description Interval E-value
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 169-282 1.59e-64

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 201.93  E-value: 1.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 169 YGGWFDDVSNYDGTTVDRTDADSVEISVGAQGNNGAFAFDPPAVRVTPGTEVTWKWTGEGGGHNVVSDGDGPLDSGGAVS 248
Cdd:TIGR03102   1 YDGFLDDVSNYDGSIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1569087971 249 EAGTTYSHTFEEMGVYKYVCVPHESLGMKGAVVV 282
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVV 114
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 32-145 8.45e-62

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 195.00  E-value: 8.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  32 YGGWFDDVSNYDG-TADKRGQDTVTITVGAQGNNGAFAFDPPAVMVSPGTEVVWEWNGEGGGHNVVSDGDGPLDSGGAVS 110
Cdd:TIGR03102   1 YDGFLDDVSNYDGsIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1569087971 111 EAGTTYSHTFESEGMFKYVCVPHEALGMKGAVVVR 145
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVVE 115
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 53-145 1.12e-37

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 131.74  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  53 TVTITVGAQGNngaFAFDPPAVMVSPGTEVVWEWNGEGGGHNVVS--DGDGPLDSGGAVSEAGTTYSHTFESEGMFKYVC 130
Cdd:cd04220     1 TVTVGVGMNGG---FAFDPAAIRVSPGTTVTWEWTGEGGGHNVVAyeDPITAFDSGSTDSSEGETYEHTFEETGEYRYVC 77

                          90
                  ....*....|....*
gi 1569087971 131 VPHEALGMKGAVVVR 145
Cdd:cd04220    78 VPHEALGMKGAIVVE 92
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 191-282 3.07e-37

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 130.58  E-value: 3.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 191 SVEISVGAQGNngaFAFDPPAVRVTPGTEVTWKWTGEGGGHNVVS--DGDGPLDSGGAVSEAGTTYSHTFEEMGVYKYVC 268
Cdd:cd04220     1 TVTVGVGMNGG---FAFDPAAIRVSPGTTVTWEWTGEGGGHNVVAyeDPITAFDSGSTDSSEGETYEHTFEETGEYRYVC 77

                          90
                  ....*....|....
gi 1569087971 269 VPHESLGMKGAVVV 282
Cdd:cd04220    78 VPHEALGMKGAIVV 91
PetE COG3794
Plastocyanin [Energy production and conversion];
205-282 3.04e-22

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 89.67  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 205 FAFDPPAVRVTPGTEVTWKWTGeGGGHNVVSDG--DGPLDSGgaVSEAGTTYSHTFEEMGVYKYVCVPHEslGMKGAVVV 282
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD-SVPHNVTSDDgpDGAFDSG--LLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVV 75
PetE COG3794
Plastocyanin [Energy production and conversion];
67-144 2.52e-20

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 84.28  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  67 FAFDPPAVMVSPGTEVVWEWNGeGGGHNVVSDG--DGPLDSGgaVSEAGTTYSHTFESEGMFKYVCVPHEalGMKGAVVV 144
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD-SVPHNVTSDDgpDGAFDSG--LLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVV 75
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
192-282 7.48e-20

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 83.96  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 192 VEISVGAQGnnGAFAFDPPAVRVTPGTEVTWKWTgEGGGHNVVSDGDG----------PLDSGGAVSEAGTTYSHTFEEM 261
Cdd:pfam00127   1 AEVLLGVDS--GDMVFEPKEITVKKGEKVTFVNN-AGMPHNVVFDKDGvpagvdadkvKMGDHTKLIGGGETYSVTFDLA 77

                          90       100
                  ....*....|....*....|.
gi 1569087971 262 GVYKYVCVPHESLGMKGAVVV 282
Cdd:pfam00127  78 GTYGFFCTPHQGAGMVGKVTV 98
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
62-144 3.47e-17

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 76.25  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  62 GNNGAFAFDPPAVMVSPGTEVVWEWNgEGGGHNVVSDGDG----------PLDSGGAVSEAGTTYSHTFESEGMFKYVCV 131
Cdd:pfam00127   7 VDSGDMVFEPKEITVKKGEKVTFVNN-AGMPHNVVFDKDGvpagvdadkvKMGDHTKLIGGGETYSVTFDLAGTYGFFCT 85

                          90
                  ....*....|...
gi 1569087971 132 PHEALGMKGAVVV 144
Cdd:pfam00127  86 PHQGAGMVGKVTV 98
SPC25 pfam06703
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
 379-401 3.78e-03

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


Pssm-ID: 461993  Cd Length: 153  Bit Score: 37.56  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|...
gi 1569087971 379 TAALVAFYFVLIALLWVFMYFVE 401
Cdd:pfam06703  54 LIVCVALYFILSGILTLWTKFVE 76
 
Name Accession Description Interval E-value
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 169-282 1.59e-64

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 201.93  E-value: 1.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 169 YGGWFDDVSNYDGTTVDRTDADSVEISVGAQGNNGAFAFDPPAVRVTPGTEVTWKWTGEGGGHNVVSDGDGPLDSGGAVS 248
Cdd:TIGR03102   1 YDGFLDDVSNYDGSIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1569087971 249 EAGTTYSHTFEEMGVYKYVCVPHESLGMKGAVVV 282
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVV 114
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 32-145 8.45e-62

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 195.00  E-value: 8.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  32 YGGWFDDVSNYDG-TADKRGQDTVTITVGAQGNNGAFAFDPPAVMVSPGTEVVWEWNGEGGGHNVVSDGDGPLDSGGAVS 110
Cdd:TIGR03102   1 YDGFLDDVSNYDGsIVDRTGQDEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTGEGGGHNVVSDGDGDLDESERVS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1569087971 111 EAGTTYSHTFESEGMFKYVCVPHEALGMKGAVVVR 145
Cdd:TIGR03102  81 EEGTTYEHTFEEPGIYLYVCVPHEALGMKGAVVVE 115
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 53-145 1.12e-37

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 131.74  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  53 TVTITVGAQGNngaFAFDPPAVMVSPGTEVVWEWNGEGGGHNVVS--DGDGPLDSGGAVSEAGTTYSHTFESEGMFKYVC 130
Cdd:cd04220     1 TVTVGVGMNGG---FAFDPAAIRVSPGTTVTWEWTGEGGGHNVVAyeDPITAFDSGSTDSSEGETYEHTFEETGEYRYVC 77

                          90
                  ....*....|....*
gi 1569087971 131 VPHEALGMKGAVVVR 145
Cdd:cd04220    78 VPHEALGMKGAIVVE 92
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 191-282 3.07e-37

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 130.58  E-value: 3.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 191 SVEISVGAQGNngaFAFDPPAVRVTPGTEVTWKWTGEGGGHNVVS--DGDGPLDSGGAVSEAGTTYSHTFEEMGVYKYVC 268
Cdd:cd04220     1 TVTVGVGMNGG---FAFDPAAIRVSPGTTVTWEWTGEGGGHNVVAyeDPITAFDSGSTDSSEGETYEHTFEETGEYRYVC 77

                          90
                  ....*....|....
gi 1569087971 269 VPHESLGMKGAVVV 282
Cdd:cd04220    78 VPHEALGMKGAIVV 91
PetE COG3794
Plastocyanin [Energy production and conversion];
205-282 3.04e-22

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 89.67  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 205 FAFDPPAVRVTPGTEVTWKWTGeGGGHNVVSDG--DGPLDSGgaVSEAGTTYSHTFEEMGVYKYVCVPHEslGMKGAVVV 282
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD-SVPHNVTSDDgpDGAFDSG--LLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVV 75
PetE COG3794
Plastocyanin [Energy production and conversion];
67-144 2.52e-20

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 84.28  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  67 FAFDPPAVMVSPGTEVVWEWNGeGGGHNVVSDG--DGPLDSGgaVSEAGTTYSHTFESEGMFKYVCVPHEalGMKGAVVV 144
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD-SVPHNVTSDDgpDGAFDSG--LLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVV 75
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
192-282 7.48e-20

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 83.96  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 192 VEISVGAQGnnGAFAFDPPAVRVTPGTEVTWKWTgEGGGHNVVSDGDG----------PLDSGGAVSEAGTTYSHTFEEM 261
Cdd:pfam00127   1 AEVLLGVDS--GDMVFEPKEITVKKGEKVTFVNN-AGMPHNVVFDKDGvpagvdadkvKMGDHTKLIGGGETYSVTFDLA 77

                          90       100
                  ....*....|....*....|.
gi 1569087971 262 GVYKYVCVPHESLGMKGAVVV 282
Cdd:pfam00127  78 GTYGFFCTPHQGAGMVGKVTV 98
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 196-281 5.23e-18

Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The Pseudocyanin-like family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind a single copper atom and are characterized by an intense electronic absorption band near 600 nm. Pseudoazurin (PAz) has been identified as a electron donor in the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. Plastocyanin is found in cyanobacteria, higher plants, and some algae where it plays a role in photosynthesis. Plastocyanin is responsible for transporting electrons from PSII to PSI. This family also includes halocyanins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis) and amicyanin found in bacteria Paracoccus denitrificans.


Pssm-ID: 259867 [Multi-domain]  Cd Length: 92  Bit Score: 78.38  E-value: 5.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 196 VGAQGNNGAFAFDPPAVRVTPGTEVTWKWTgEGGGHNVVSDgDGPLDSGGAVSEA------GTTYSHTFEEMGVYKYVCV 269
Cdd:cd04204     3 VKMGADNGAMAFEPAAIRVDAGETVEFVNT-GGGPHNVVFD-KEIVPDGDAEFESdrvdeeGFTYEQTFDEPGVYGYYCT 80

                          90
                  ....*....|..
gi 1569087971 270 PHESLGMKGAVV 281
Cdd:cd04204    81 PHRGAGMVGTVI 92
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
62-144 3.47e-17

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 76.25  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  62 GNNGAFAFDPPAVMVSPGTEVVWEWNgEGGGHNVVSDGDG----------PLDSGGAVSEAGTTYSHTFESEGMFKYVCV 131
Cdd:pfam00127   7 VDSGDMVFEPKEITVKKGEKVTFVNN-AGMPHNVVFDKDGvpagvdadkvKMGDHTKLIGGGETYSVTFDLAGTYGFFCT 85

                          90
                  ....*....|...
gi 1569087971 132 PHEALGMKGAVVV 144
Cdd:pfam00127  86 PHQGAGMVGKVTV 98
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 58-143 9.45e-17

Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The Pseudocyanin-like family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind a single copper atom and are characterized by an intense electronic absorption band near 600 nm. Pseudoazurin (PAz) has been identified as a electron donor in the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. Plastocyanin is found in cyanobacteria, higher plants, and some algae where it plays a role in photosynthesis. Plastocyanin is responsible for transporting electrons from PSII to PSI. This family also includes halocyanins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis) and amicyanin found in bacteria Paracoccus denitrificans.


Pssm-ID: 259867 [Multi-domain]  Cd Length: 92  Bit Score: 74.91  E-value: 9.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  58 VGAQGNNGAFAFDPPAVMVSPGTEVVWEWNgEGGGHNVVSDgDGPLDSGGAVSEA------GTTYSHTFESEGMFKYVCV 131
Cdd:cd04204     3 VKMGADNGAMAFEPAAIRVDAGETVEFVNT-GGGPHNVVFD-KEIVPDGDAEFESdrvdeeGFTYEQTFDEPGVYGYYCT 80

                          90
                  ....*....|..
gi 1569087971 132 PHEALGMKGAVV 143
Cdd:cd04204    81 PHRGAGMVGTVI 92
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 200-282 1.61e-13

Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI; Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI.


Pssm-ID: 259881 [Multi-domain]  Cd Length: 97  Bit Score: 65.85  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 200 GNNGAFAFDPPAVRVTPGTEVTWKwTGEGGGHNVVSDGD--GPLDSGGAVS------EAGTTYSHTFEEMGVYKYVCVPH 271
Cdd:cd04219     7 SDSGALVFEPKELTVKAGDTVEFV-NNKGGPHNVVFDEDavPSAVDAAALShkdllnAPGETFSVTFPAPGTYTFYCEPH 85

                          90
                  ....*....|.
gi 1569087971 272 ESLGMKGAVVV 282
Cdd:cd04219    86 RGAGMVGKITV 96
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 67-145 1.61e-13

Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.


Pssm-ID: 259988 [Multi-domain]  Cd Length: 81  Bit Score: 65.43  E-value: 1.61e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1569087971  67 FAFDPPAVMVSPGTEVVWEwNGEGGGHNVVSDgDGPLDSGGAvsEAGTTYSHTFESEGMFKYVCVPHEAlgMKGAVVVR 145
Cdd:cd13921     9 FKFNPAEVTVKVGDTVTWT-NKDSVPHTVTAE-DGAFDSGML--ATGKSFSYTFTAAGTYDYFCTIHPF--MKGTVTVE 81
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 54-144 3.67e-13

Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI; Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI.


Pssm-ID: 259881 [Multi-domain]  Cd Length: 97  Bit Score: 65.08  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  54 VTITVGAqgNNGAFAFDPPAVMVSPGTEVVWEwNGEGGGHNVVSDGD--GPLDSGGAVS------EAGTTYSHTFESEGM 125
Cdd:cd04219     1 ATVKMGS--DSGALVFEPKELTVKAGDTVEFV-NNKGGPHNVVFDEDavPSAVDAAALShkdllnAPGETFSVTFPAPGT 77

                          90
                  ....*....|....*....
gi 1569087971 126 FKYVCVPHEALGMKGAVVV 144
Cdd:cd04219    78 YTFYCEPHRGAGMVGKITV 96
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 205-282 1.38e-12

Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.


Pssm-ID: 259988 [Multi-domain]  Cd Length: 81  Bit Score: 62.73  E-value: 1.38e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1569087971 205 FAFDPPAVRVTPGTEVTWKwTGEGGGHNVVSDgDGPLDSGGAvsEAGTTYSHTFEEMGVYKYVCVPHESlgMKGAVVV 282
Cdd:cd13921     9 FKFNPAEVTVKVGDTVTWT-NKDSVPHTVTAE-DGAFDSGML--ATGKSFSYTFTAAGTYDYFCTIHPF--MKGTVTV 80
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 200-282 1.83e-10

Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has been identified as an electron donor to the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. It has been shown that pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of the product nitric oxide. The ability of this small redox protein to interact with a multitude of structurally different partners has been attributed to the hydrophobic character of the binding surface.


Pssm-ID: 259880 [Multi-domain]  Cd Length: 117  Bit Score: 58.08  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971 200 GNNGAFAFDPPAVRVTPGTEVTWKWTGegGGHNVVS-DGDGPLDSGGAVSEAGTTYSHTFEEMGVYKYVCVPHESLGMKG 278
Cdd:cd04218    10 GAGGAMVFEPAFLRAEPGDTVTFVPTD--KSHNAASiKGMLPEGAEPFKGKINEEITVTFEKEGVYGYKCTPHYGMGMVG 87


                  ....
gi 1569087971 279 AVVV 282
Cdd:cd04218    88 LIQV 91
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 62-144 4.32e-07

Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has been identified as an electron donor to the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. It has been shown that pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of the product nitric oxide. The ability of this small redox protein to interact with a multitude of structurally different partners has been attributed to the hydrophobic character of the binding surface.


Pssm-ID: 259880 [Multi-domain]  Cd Length: 117  Bit Score: 48.45  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  62 GNNGAFAFDPPAVMVSPGTEVvwEWNGEGGGHNVVS-DGDGPLDSGGAVSEAGTTYSHTFESEGMFKYVCVPHEALGMKG 140
Cdd:cd04218    10 GAGGAMVFEPAFLRAEPGDTV--TFVPTDKSHNAASiKGMLPEGAEPFKGKINEEITVTFEKEGVYGYKCTPHYGMGMVG 87


                  ....
gi 1569087971 141 AVVV 144
Cdd:cd04218    88 LIQV 91
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 53-140 1.92e-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: 37.60  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569087971  53 TVTITVGAQGNNGAFAFDPPAVMVSPGTEVVWE-WNGEGGGHNVV-----------SDGDGPLDSGGAVSEAGTTYSHTF 120
Cdd:cd00920     4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQfVNKLGENHSVTiagfgvpvvamAGGANPGLVNTLVIGPGESAEVTF 83

                          90       100
                  ....*....|....*....|....
gi 1569087971 121 --ESEGMFKYVC--VPHEALGMKG 140
Cdd:cd00920    84 ttDQAGVYWFYCtiPGHNHAGMVG 107
SPC25 pfam06703
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
 379-401 3.78e-03

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


Pssm-ID: 461993  Cd Length: 153  Bit Score: 37.56  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|...
gi 1569087971 379 TAALVAFYFVLIALLWVFMYFVE 401
Cdd:pfam06703  54 LIVCVALYFILSGILTLWTKFVE 76
 
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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