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Conserved domains on  [gi|3929319|gb|AAC79870|]
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putative copper/zinc superoxide dismutase copper chaperone, partial [Dendrobium hybrid cultivar]

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
10-119 1.87e-64

copper, zinc superoxide dismutase


The actual alignment was detected with superfamily member PLN02957:

Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 195.74  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3929319    10 LDEFMVDMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKTMLKALEQTGRNARLIGQGNPNDFLVSSAVAE 89
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 3929319    90 FKGPVIFGVVRLAQVNMELSRIEASFSGLS 119
Cdd:PLN02957  87 FKGPDIFGVVRFAQVSMELARIEAAFSGLS 116
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
10-119 1.87e-64

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 195.74  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3929319    10 LDEFMVDMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKTMLKALEQTGRNARLIGQGNPNDFLVSSAVAE 89
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 3929319    90 FKGPVIFGVVRLAQVNMELSRIEASFSGLS 119
Cdd:PLN02957  87 FKGPDIFGVVRFAQVSMELARIEAAFSGLS 116
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
12-71 2.68e-15

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: 65.32  E-value: 2.68e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929319   12 EFMVD-MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIG--SVPVKTMLKALEQTGRNAR 71
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
16-67 2.21e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 55.30  E-value: 2.21e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929319   16 DMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGS---VPVKTMLKALEQTG 67
Cdd:COG2608  10 GMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAG 64
HMA pfam00403
Heavy-metal-associated domain;
13-58 2.93e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.84  E-value: 2.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 3929319     13 FMVDMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKT 58
Cdd:pfam00403   3 RVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTK 48
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
17-70 1.65e-04

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 38.09  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 3929319     17 MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSvPVKTMLKALEQTGRNA 70
Cdd:TIGR02052  32 MTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFD-DEKTNVKALTEATTDA 84
 
Name Accession Description Interval E-value
PLN02957 PLN02957
copper, zinc superoxide dismutase
10-119 1.87e-64

copper, zinc superoxide dismutase


Pssm-ID: 215516 [Multi-domain]  Cd Length: 238  Bit Score: 195.74  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3929319    10 LDEFMVDMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKTMLKALEQTGRNARLIGQGNPNDFLVSSAVAE 89
Cdd:PLN02957   7 LTEFMVDMKCEGCVAAVKNKLETLEGVKAVEVDLSNQVVRVLGSSPVKAMTAALEQTGRKARLIGQGDPEDFLVSAAVAE 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 3929319    90 FKGPVIFGVVRLAQVNMELSRIEASFSGLS 119
Cdd:PLN02957  87 FKGPDIFGVVRFAQVSMELARIEAAFSGLS 116
HMA cd00371
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ...
12-71 2.68e-15

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: 65.32  E-value: 2.68e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929319   12 EFMVD-MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIG--SVPVKTMLKALEQTGRNAR 71
Cdd:cd00371   1 ELSVEgMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYdpEVSPEELLEAIEDAGYKAR 63
CopZ COG2608
Copper chaperone CopZ [Inorganic ion transport and metabolism];
16-67 2.21e-11

Copper chaperone CopZ [Inorganic ion transport and metabolism];


Pssm-ID: 442020 [Multi-domain]  Cd Length: 71  Bit Score: 55.30  E-value: 2.21e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929319   16 DMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGS---VPVKTMLKALEQTG 67
Cdd:COG2608  10 GMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYDpekVSLEDIKAAIEEAG 64
HMA pfam00403
Heavy-metal-associated domain;
13-58 2.93e-08

Heavy-metal-associated domain;


Pssm-ID: 459804 [Multi-domain]  Cd Length: 58  Bit Score: 46.84  E-value: 2.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 3929319     13 FMVDMTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKT 58
Cdd:pfam00403   3 RVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTVTGDAESTK 48
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
12-104 4.22e-07

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


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 47.06  E-value: 4.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3929319   12 EFMVD-MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVI---GSVPVKTMLKALEQTGRNARLIGQGNPNDFLVSSAV 87
Cdd:COG2217   4 RLRIEgMTCAACAWLIEKALRKLPGVLSARVNLATERARVEydpGKVSLEELIAAVEKAGYEAEPADADAAAEEAREKEL 83
                        90
                ....*....|....*..
gi 3929319   88 AEFKGPVIFGVVRLAQV 104
Cdd:COG2217  84 RDLLRRLAVAGVLALPV 100
copA PRK10671
copper-exporting P-type ATPase CopA;
17-73 1.26e-05

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 43.19  E-value: 1.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 3929319    17 MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVPVKTMLKALEQTGRNARLI 73
Cdd:PRK10671 108 MSCASCVSRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEAI 164
PRK13748 PRK13748
putative mercuric reductase; Provisional
17-72 5.97e-05

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 40.91  E-value: 5.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 3929319    17 MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVI--GSVPVKTMLKALEQTGRNARL 72
Cdd:PRK13748   9 MTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAieVGTSPDALTAAVAGLGYRATL 66
MerP TIGR02052
mercuric transport protein periplasmic component; This model represents the periplasmic ...
17-70 1.65e-04

mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]


Pssm-ID: 131107 [Multi-domain]  Cd Length: 92  Bit Score: 38.09  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 3929319     17 MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSvPVKTMLKALEQTGRNA 70
Cdd:TIGR02052  32 MTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFD-DEKTNVKALTEATTDA 84
TIGR00003 TIGR00003
copper ion binding protein; This model describes an apparently copper-specific subfamily of ...
17-70 8.64e-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: 35.59  E-value: 8.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 3929319     17 MTCEGCVSAVKNSMLKLDGVSGVDVDLSNQLVRVIGSVP---VKTMLKALEQTGRNA 70
Cdd:TIGR00003   9 MSCNHCVDKIEKFVGEIEGVSKVKVQLEKEKVVVEFDAPnvsATEICEAILDAGYEV 65
 
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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