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Conserved domains on  [gi|387763015|ref|NP_001248444|]
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copper chaperone for superoxide dismutase [Macaca mulatta]

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
 14-253 2.30e-70

copper, zinc superoxide dismutase


The actual alignment was detected with superfamily member PLN02957:

Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 216.93  E-value: 2.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  14 LEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSDQLHNLGAAVAIL 93
Cdd:PLN02957   8 TEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAEF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  94 GGPgTVQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNP-DGASHGGPQdsdrhrGDLGNVH 172
Cdd:PLN02957  88 KGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015 173 ADADGCAIFRMEDEKLKVWDVIGRSLVIDEGEDdlgrgghplskitgNSGQRLACGIIARSAGLFQNPKQICSCDGLTIW 252
Cdd:PLN02957 161 ADENGEATFSGTKEKLKVWDLIGRSLAVYATAD--------------KSGPGIAAAVIARSAGVGENYKKLCSCDGTVIW 226


                 .
gi 387763015 253 E 253
Cdd:PLN02957 227 E 227
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
 14-253 2.30e-70

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 216.93  E-value: 2.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  14 LEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSDQLHNLGAAVAIL 93
Cdd:PLN02957   8 TEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAEF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  94 GGPgTVQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNP-DGASHGGPQdsdrhrGDLGNVH 172
Cdd:PLN02957  88 KGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015 173 ADADGCAIFRMEDEKLKVWDVIGRSLVIDEGEDdlgrgghplskitgNSGQRLACGIIARSAGLFQNPKQICSCDGLTIW 252
Cdd:PLN02957 161 ADENGEATFSGTKEKLKVWDLIGRSLAVYATAD--------------KSGPGIAAAVIARSAGVGENYKKLCSCDGTVIW 226


                 .
gi 387763015 253 E 253
Cdd:PLN02957 227 E 227
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 89-227 1.35e-53

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: 170.52  E-value: 1.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAIL-GGPGTVQGVVRFLQlSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGD 167
Cdd:cd00305    3 AVAVLkGPDGKVVGTVTFTQ-QSGGVTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHAGD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387763015 168 LGNVHADADGCAIFRMEDEKLKVW---DVIGRSLVIDEGEDDLGRGGHPLSKITGNSGQRLAC 227
Cdd:cd00305   82 LGNIVADKDGVATVSVLDPLISLKggnSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 99-230 8.68e-52

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: 165.43  E-value: 8.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015   99 VQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGDLGNVHADADGC 178
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 387763015  179 AIFRMEDEKLKVWD---VIGRSLVIDEGEDDLGRgghplsKITGNSGQRLACGII 230
Cdd:pfam00080  81 ATVEFTDSLISLSGgnsIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
89-233 4.28e-35

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


Pssm-ID: 441635  Cd Length: 171  Bit Score: 123.82  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAILGGPGTVQGVVRFLQlSPERCLIEGTIDGLESGLHGLHVHQYGDltnnCN-----SCGDHFNPDGASHGGPQDSDR 163
Cdd:COG2032   30 ATLVDTGDGKVVGTVTFTE-TPGGVLVTVELSGLPPGEHGFHIHEKGD----CSapdfkSAGGHFNPTGTKHGGPNPDGP 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387763015 164 HRGDLGNVHADADGCAIFRMEDEKLKVW---DVIGRSLVIDEGEDDLgrGGHPlskiTGNSGQRLACGIIARS 233
Cdd:COG2032  105 HAGDLPNLYVDADGTATLEVLAPRLTLGglnDLDGRALIIHAGPDDY--STQP----SGNAGARIACGVIKAA 171
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 20-53 7.65e-07

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 45.55  E-value: 7.65e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 387763015  20 MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLV 53
Cdd:NF033795   9 MSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDV 42
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 15-67 3.10e-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: 38.29  E-value: 3.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 387763015   15 EFAVQ-MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLE 67
Cdd:TIGR00003   3 TFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICE 56
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
 14-253 2.30e-70

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 216.93  E-value: 2.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  14 LEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSDQLHNLGAAVAIL 93
Cdd:PLN02957   8 TEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAEF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  94 GGPgTVQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNP-DGASHGGPQdsdrhrGDLGNVH 172
Cdd:PLN02957  88 KGP-DIFGVVRFAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPsDDDTDEEPL------GDLGTLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015 173 ADADGCAIFRMEDEKLKVWDVIGRSLVIDEGEDdlgrgghplskitgNSGQRLACGIIARSAGLFQNPKQICSCDGLTIW 252
Cdd:PLN02957 161 ADENGEATFSGTKEKLKVWDLIGRSLAVYATAD--------------KSGPGIAAAVIARSAGVGENYKKLCSCDGTVIW 226


                 .
gi 387763015 253 E 253
Cdd:PLN02957 227 E 227
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 89-227 1.35e-53

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: 170.52  E-value: 1.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAIL-GGPGTVQGVVRFLQlSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGD 167
Cdd:cd00305    3 AVAVLkGPDGKVVGTVTFTQ-QSGGVTITGELSGLTPGLHGFHIHEFGDCTNGCTSAGGHFNPFGKKHGGPNDEGRHAGD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387763015 168 LGNVHADADGCAIFRMEDEKLKVW---DVIGRSLVIDEGEDDLGRGGHPLSKITGNSGQRLAC 227
Cdd:cd00305   82 LGNIVADKDGVATVSVLDPLISLKggnSIIGRSLVVHAGQDDLGKGPDELSGGTGNAGVRVAC 144
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 99-230 8.68e-52

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: 165.43  E-value: 8.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015   99 VQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGDLGNVHADADGC 178
Cdd:pfam00080   1 VSGTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGHFNPTGKQHGGPNDDGRHVGDLGNITADADGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 387763015  179 AIFRMEDEKLKVWD---VIGRSLVIDEGEDDLGRgghplsKITGNSGQRLACGII 230
Cdd:pfam00080  81 ATVEFTDSLISLSGgnsIIGRALVVHAGPDDLGT------QPTGNAGARIACGVI 129
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
 89-230 7.94e-42

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 140.81  E-value: 7.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAILGGPGTVQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGDL 168
Cdd:PLN02386   4 AVAVLNSSEGVKGTIFFTQEGDGPTTVTGSLSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGDL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387763015 169 GNVHADADGCAIFRMEDEKLKVW---DVIGRSLVIDEGEDDLGRGGHPLSKITGNSGQRLACGII 230
Cdd:PLN02386  84 GNVTVGDDGTATFTIVDKQIPLTgpnSIVGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGII 148
PLN02642 PLN02642
copper, zinc superoxide dismutase
 89-231 1.71e-36

copper, zinc superoxide dismutase


Pssm-ID: 178248  Cd Length: 164  Bit Score: 127.51  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAILGGPGTVQGVVRFLQLSPERCLIEGTIDGLESGLHGLHVHQYGDLTNNCNSCGDHFNPDGASHGGPQDSDRHRGDL 168
Cdd:PLN02642  10 AVALIAGDNNVRGCLQFVQDIFGTTHVTGKISGLSPGFHGFHIHSFGDTTNGCISTGPHFNPLNRVHGPPNEEERHAGDL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 387763015 169 GNVHADADGCAIFRMEDEKLKV---WDVIGRSLVIDEGEDDLGRGGHPLSKITGNSGQRLACGIIA 231
Cdd:PLN02642  90 GNILAGSDGVAEILIKDKHIPLsgqYSILGRAVVVHADPDDLGKGGHKLSKSTGNAGSRVGCGIIG 155
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
89-233 4.28e-35

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


Pssm-ID: 441635  Cd Length: 171  Bit Score: 123.82  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  89 AVAILGGPGTVQGVVRFLQlSPERCLIEGTIDGLESGLHGLHVHQYGDltnnCN-----SCGDHFNPDGASHGGPQDSDR 163
Cdd:COG2032   30 ATLVDTGDGKVVGTVTFTE-TPGGVLVTVELSGLPPGEHGFHIHEKGD----CSapdfkSAGGHFNPTGTKHGGPNPDGP 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387763015 164 HRGDLGNVHADADGCAIFRMEDEKLKVW---DVIGRSLVIDEGEDDLgrGGHPlskiTGNSGQRLACGIIARS 233
Cdd:COG2032  105 HAGDLPNLYVDADGTATLEVLAPRLTLGglnDLDGRALIIHAGPDDY--STQP----SGNAGARIACGVIKAA 171
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
 15-73 5.84e-13

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: 62.24  E-value: 5.84e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387763015  15 EFAVQ-MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHT--TLPSQEVQALLEGTGRQA 73
Cdd:cd00371    1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKA 62
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
13-76 1.23e-10

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 56.07  E-value: 1.23e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387763015  13 TLEFAVQ-MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVH---TTLPSQEVQALLEGTGRQAVLK 76
Cdd:COG2608    3 TVTLKVEgMTCGHCVARVEKALKALDGVASVEVDLATGTATVTydpEKVSLEDIKAAIEEAGYEVEKA 70
PRK15388 PRK15388
superoxide dismutase [Cu-Zn];
95-232 8.06e-09

superoxide dismutase [Cu-Zn];


Pssm-ID: 185286  Cd Length: 177  Bit Score: 53.93  E-value: 8.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  95 GPGTVQGVVRFLQlSPERCLIEGTIDGLESGLHGLHVHQ----YGDLTNNCN----SCGDHFNP-DGASHGGPQDSDRHR 165
Cdd:PRK15388  35 GTGENIGEITVSE-TPYGLLFTPHLNGLTPGIHGFHVHTnpscMPGMKDGKEvpalMAGGHLDPeKTGKHLGPYNDKGHL 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387763015 166 GDLGNVHADADGCAIFRMEDEKLK-VWDVIGRSLVIDEGEDDLGRGGHPLskitGNSGQRLACGIIAR 232
Cdd:PRK15388 114 GDLPGLVVNADGTATYPLLAPRLKsLSELKGHSLMIHKGGDNYSDKPAPL----GGGGARFACGVIEK 177
HMA pfam00403
Heavy-metal-associated domain;
16-67 1.42e-07

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 47.23  E-value: 1.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 387763015   16 FAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLE 67
Cdd:pfam00403   3 RVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTKLEKLVE 54
chaper_CopZ_Bs NF033795
copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in ...
 20-53 7.65e-07

copper chaperone CopZ; This model describes CopZ, a small copper chaperone, as found in Bacillus subtilis and related species. A number of longer protein, such as copper-translocating P-type ATPases, contain multiple CopZ-like domains, with its signature invariant CxxC motif. CopZ from other species may be more different in sequence from this family than some of those domains of longer proteins.


Pssm-ID: 411375 [Multi-domain]  Cd Length: 66  Bit Score: 45.55  E-value: 7.65e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 387763015  20 MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLV 53
Cdd:NF033795   9 MSCGHCVKAVEGALGELNGVSSVKVNLEEGKVDV 42
PRK10290 PRK10290
superoxide dismutase [Cu-Zn] SodC2;
119-230 6.85e-06

superoxide dismutase [Cu-Zn] SodC2;


Pssm-ID: 182357 [Multi-domain]  Cd Length: 173  Bit Score: 45.22  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015 119 IDGLESGLHGLHVHQYGDL--------TNNCNSCGDHFNP-DGASHGGPqDSDRHRGDLGNVHADADGCAIFRMEDEKLK 189
Cdd:PRK10290  56 LKALPPGEHGFHIHAKGSCqpatkdgkASAAEAAGGHLDPqNTGKHEGP-EGAGHLGDLPALVVNNDGKATDPVIAPRLK 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 387763015 190 VWD-VIGRSLVIDEGEDDLGRGGHPLskitGNSGQRLACGII 230
Cdd:PRK10290 135 SLDeVKDKALMVHVGGDNMSDQPKPL----GGGGERYACGVI 172
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
13-96 2.02e-05

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 45.52  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  13 TLEFAVQ-MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVH---TTLPSQEVQALLEGTGRQAVLKGMGS-------- 80
Cdd:COG2217    2 RVRLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPADADAaaeearek 81

                         90
                 ....*....|....*....
gi 387763015  81 ---DQLHNLGAAvAILGGP 96
Cdd:COG2217   82 elrDLLRRLAVA-GVLALP 99
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
 15-67 3.10e-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: 38.29  E-value: 3.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 387763015   15 EFAVQ-MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTTLPSQEVQALLE 67
Cdd:TIGR00003   3 TFQVKgMSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPNVSATEICE 56
copA PRK10671
copper-exporting P-type ATPase CopA;
20-64 8.72e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 40.49  E-value: 8.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 387763015  20 MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVH-TTLPSQEVQA 64
Cdd:PRK10671 108 MSCASCVSRVQNALQSVPGVTQARVNLAERTALVMgSASPQDLVQA 153
PRK13748 PRK13748
putative mercuric reductase; Provisional
 20-121 4.35e-03

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 38.21  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763015  20 MTCQSCVDAVRKSLQGVAGVQDVEVHLENQMVLVHTT--LPSQEVQALLEGTGRQAVLK--------------------- 76
Cdd:PRK13748   9 MTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEvgTSPDALTAAVAGLGYRATLAdapptdnrgglldkmrgwlgg 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 387763015  77 ----GMGSDQLHnlgaaVAILG-GPGTVQGVVRFLQLSPERCLIE-GTIDG 121
Cdd:PRK13748  89 adkhSGNERPLH-----VAVIGsGGAAMAAALKAVEQGARVTLIErGTIGG 134
 
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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