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Conserved domains on  [gi|16758084|ref|NP_445877|]
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copper chaperone for superoxide dismutase [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02957 super family cl33606
copper, zinc superoxide dismutase
 13-253 1.18e-69

copper, zinc superoxide dismutase


The actual alignment was detected with superfamily member PLN02957:

Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 215.00  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   13 ALEFTVQMSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLESTGRQAVLKGMGSSQLKNLGAAVAI 92
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   93 MEGSgTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNP-DGASHGGPQdtdrhrGDLGNV 171
Cdd:PLN02957  87 FKGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  172 HAEASGRATFRIEDKQLKVWDVIGRSLVVDEGEDDLGRGGhplskvtgnsgkrlACGIIARSAGLFQNPKQICSCDGLTI 251
Cdd:PLN02957 160 EADENGEATFSGTKEKLKVWDLIGRSLAVYATADKSGPGI--------------AAAVIARSAGVGENYKKLCSCDGTVI 225


                 ..
gi 16758084  252 WE 253
Cdd:PLN02957 226 WE 227
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
 13-253 1.18e-69

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 215.00  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   13 ALEFTVQMSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLESTGRQAVLKGMGSSQLKNLGAAVAI 92
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   93 MEGSgTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNP-DGASHGGPQdtdrhrGDLGNV 171
Cdd:PLN02957  87 FKGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  172 HAEASGRATFRIEDKQLKVWDVIGRSLVVDEGEDDLGRGGhplskvtgnsgkrlACGIIARSAGLFQNPKQICSCDGLTI 251
Cdd:PLN02957 160 EADENGEATFSGTKEKLKVWDLIGRSLAVYATADKSGPGI--------------AAAVIARSAGVGENYKKLCSCDGTVI 225


                 ..
gi 16758084  252 WE 253
Cdd:PLN02957 226 WE 227
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 99-230 3.72e-56

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 176.60  E-value: 3.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084    99 VQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGDLGNVHAEASGR 178
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16758084   179 ATFRIEDKQLKVWD---VIGRSLVVDEGEDDLGRgghplsKVTGNSGKRLACGII 230
Cdd:pfam00080  81 ATVEFTDSLISLSGgnsIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 89-227 5.14e-56

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 176.68  E-value: 5.14e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  89 AVAIMEG-SGTVQGVVRFLQlSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGD 167
Cdd:cd00305   3 AVAVLKGpDGKVVGTVTFTQ-QSGGVTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHAGD 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758084 168 LGNVHAEASGRATFRIEDKQLKVW---DVIGRSLVVDEGEDDLGRGGHPLSKVTGNSGKRLAC 227
Cdd:cd00305  82 LGNIVADKDGVATVSVLDPLISLKggnSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
89-233 5.32e-38

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 131.53  E-value: 5.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  89 AVAIME--GSGTVQGVVRFLQLSSELcLIEGTIDGLEPGLHGLHVHQYGDLT-KDCSSCGDHFNPDGASHGGPQDTDRHR 165
Cdd:COG2032  28 ATATLVdtGDGKVVGTVTFTETPGGV-LVTVELSGLPPGEHGFHIHEKGDCSaPDFKSAGGHFNPTGTKHGGPNPDGPHA 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758084 166 GDLGNVHAEASGRATFRIEDKQLKVW---DVIGRSLVVDEGEDDLgrGGHPlskvTGNSGKRLACGIIARS 233
Cdd:COG2032 107 GDLPNLYVDADGTATLEVLAPRLTLGglnDLDGRALIIHAGPDDY--STQP----SGNAGARIACGVIKAA 171
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 15-68 4.08e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 37.91  E-value: 4.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16758084    15 EFTVQ-MSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLES 68
Cdd:TIGR00003   3 TFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEA 57
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
 13-253 1.18e-69

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 215.00  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   13 ALEFTVQMSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLESTGRQAVLKGMGSSQLKNLGAAVAI 92
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   93 MEGSgTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNP-DGASHGGPQdtdrhrGDLGNV 171
Cdd:PLN02957  87 FKGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  172 HAEASGRATFRIEDKQLKVWDVIGRSLVVDEGEDDLGRGGhplskvtgnsgkrlACGIIARSAGLFQNPKQICSCDGLTI 251
Cdd:PLN02957 160 EADENGEATFSGTKEKLKVWDLIGRSLAVYATADKSGPGI--------------AAAVIARSAGVGENYKKLCSCDGTVI 225


                 ..
gi 16758084  252 WE 253
Cdd:PLN02957 226 WE 227
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 99-230 3.72e-56

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 176.60  E-value: 3.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084    99 VQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGDLGNVHAEASGR 178
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16758084   179 ATFRIEDKQLKVWD---VIGRSLVVDEGEDDLGRgghplsKVTGNSGKRLACGII 230
Cdd:pfam00080  81 ATVEFTDSLISLSGgnsIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 89-227 5.14e-56

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 176.68  E-value: 5.14e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  89 AVAIMEG-SGTVQGVVRFLQlSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGD 167
Cdd:cd00305   3 AVAVLKGpDGKVVGTVTFTQ-QSGGVTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHAGD 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758084 168 LGNVHAEASGRATFRIEDKQLKVW---DVIGRSLVVDEGEDDLGRGGHPLSKVTGNSGKRLAC 227
Cdd:cd00305  82 LGNIVADKDGVATVSVLDPLISLKggnSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
 89-230 1.37e-43

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 145.44  E-value: 1.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   89 AVAIMEGSGTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGDL 168
Cdd:PLN02386   4 AVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGDL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758084  169 GNVHAEASGRATFRIEDKQLKVW---DVIGRSLVVDEGEDDLGRGGHPLSKVTGNSGKRLACGII 230
Cdd:PLN02386  84 GNVTVGDDGTATFTIVDKQIPLTgpnSIVGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGII 148
PLN02642 PLN02642
copper, zinc superoxide dismutase
 89-231 3.84e-39

copper, zinc superoxide dismutase


Pssm-ID: 178248  Cd Length: 164  Bit Score: 134.44  E-value: 3.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   89 AVAIMEGSGTVQGVVRFLQLSSELCLIEGTIDGLEPGLHGLHVHQYGDLTKDCSSCGDHFNPDGASHGGPQDTDRHRGDL 168
Cdd:PLN02642  10 AVALIAGDNNVRGCLQFVQDIFGTTHVTGKISGLSPGFHGFHIHSFGDTTNGCISTGPHFNPLNRVHGPPNEEERHAGDL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758084  169 GNVHAEASGRATFRIEDKQLKV---WDVIGRSLVVDEGEDDLGRGGHPLSKVTGNSGKRLACGIIA 231
Cdd:PLN02642  90 GNILAGSDGVAEILIKDKHIPLsgqYSILGRAVVVHADPDDLGKGGHKLSKSTGNAGSRVGCGIIG 155
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
89-233 5.32e-38

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 131.53  E-value: 5.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  89 AVAIME--GSGTVQGVVRFLQLSSELcLIEGTIDGLEPGLHGLHVHQYGDLT-KDCSSCGDHFNPDGASHGGPQDTDRHR 165
Cdd:COG2032  28 ATATLVdtGDGKVVGTVTFTETPGGV-LVTVELSGLPPGEHGFHIHEKGDCSaPDFKSAGGHFNPTGTKHGGPNPDGPHA 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758084 166 GDLGNVHAEASGRATFRIEDKQLKVW---DVIGRSLVVDEGEDDLgrGGHPlskvTGNSGKRLACGIIARS 233
Cdd:COG2032 107 GDLPNLYVDADGTATLEVLAPRLTLGglnDLDGRALIIHAGPDDY--STQP----SGNAGARIACGVIKAA 171
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 15-73 3.14e-10

Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.


Pssm-ID: 238219 [Multi-domain]  Cd Length: 63  Bit Score: 54.92  E-value: 3.14e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758084  15 EFTVQ-MSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQT--TLPSQEVQALLESTGRQA 73
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKA 62
PRK15388 PRK15388
superoxide dismutase [Cu-Zn];
95-232 4.45e-09

superoxide dismutase [Cu-Zn];


Pssm-ID: 185286  Cd Length: 177  Bit Score: 54.70  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084   95 GSGTVQGVVRFLQLSSELcLIEGTIDGLEPGLHGLHVHQYGDLTKDCSS--------CGDHFNP-DGASHGGPQDTDRHR 165
Cdd:PRK15388  35 GTGENIGEITVSETPYGL-LFTPHLNGLTPGIHGFHVHTNPSCMPGMKDgkevpalmAGGHLDPeKTGKHLGPYNDKGHL 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758084  166 GDLGNVHAEASGRATFRIEDKQLK-VWDVIGRSLVVDEGEDDLGRGGHPLskvtGNSGKRLACGIIAR 232
Cdd:PRK15388 114 GDLPGLVVNADGTATYPLLAPRLKsLSELKGHSLMIHKGGDNYSDKPAPL----GGGGARFACGVIEK 177
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
14-76 8.40e-09

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 51.06  E-value: 8.40e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758084  14 LEFTVQ-MSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQ---TTLPSQEVQALLESTGRQAVLK 76
Cdd:COG2608   4 VTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTydpEKVSLEDIKAAIEEAGYEVEKA 70
PRK10290 PRK10290
superoxide dismutase [Cu-Zn] SodC2;
119-230 1.23e-07

superoxide dismutase [Cu-Zn] SodC2;


Pssm-ID: 182357 [Multi-domain]  Cd Length: 173  Bit Score: 50.61  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758084  119 IDGLEPGLHGLHVHQYGDL---TKD-----CSSCGDHFNP-DGASHGGPqDTDRHRGDLGNVHAEASGRATFRIEDKQLK 189
Cdd:PRK10290  56 LKALPPGEHGFHIHAKGSCqpaTKDgkasaAEAAGGHLDPqNTGKHEGP-EGAGHLGDLPALVVNNDGKATDPVIAPRLK 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16758084  190 VWD-VIGRSLVVDEGEDDLGRGGHPLskvtGNSGKRLACGII 230
Cdd:PRK10290 135 SLDeVKDKALMVHVGGDNMSDQPKPL----GGGGERYACGVI 172
HMA pfam00403
Heavy-metal-associated domain;
18-68 2.50e-05

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 41.07  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16758084    18 VQMSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLES 68
Cdd:pfam00403   5 SGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVEA 55
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 15-68 4.08e-04

copper ion binding protein; This model describes an apparently copper-specific subfamily of the metal-binding domain HMA (pfam00403). Closely related sequences outside this model include mercury resistance proteins and repeated domains of eukaryotic eukaryotic copper transport proteins. Members of this family are strictly prokaryotic. The model identifies both small proteins consisting of just this domain and N-terminal regions of cation (probably copper) transporting ATPases. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 188014 [Multi-domain]  Cd Length: 66  Bit Score: 37.91  E-value: 4.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16758084    15 EFTVQ-MSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQTTLPSQEVQALLES 68
Cdd:TIGR00003   3 TFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICEA 57
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
14-75 8.19e-03

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 37.43  E-value: 8.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758084  14 LEFTVQ-MSCQSCVDAVHKTLKGAAGVQNVEVQLENQMVLVQ---TTLPSQEVQALLESTGRQAVL 75
Cdd:COG2217   3 VRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEP 68
 
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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