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Conserved domains on  [gi|328774125|gb|EGF84162|]
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hypothetical protein BATDEDRAFT_84890 [Batrachochytrium dendrobatidis JAM81]

Protein Classification

copper transporter family protein( domain architecture ID 10514254)

copper transporter (Ctr) family protein such as human high affinity copper uptake protein 1 and Cryptococcus neoformans copper transport protein CTR4, which are both involved in high affinity copper uptake

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ctr pfam04145
Ctr copper transporter family; The redox active metal copper is an essential cofactor in ...
290-554 4.89e-24

Ctr copper transporter family; The redox active metal copper is an essential cofactor in critical biological processes such as respiration, iron transport, oxidative stress protection, hormone production, and pigmentation. A widely conserved family of high-affinity copper transport proteins (Ctr proteins) mediates copper uptake at the plasma membrane. A series of clustered methionine residues in the hydrophilic extracellular domain, and an MXXXM motif in the second transmembrane domain, are important for copper uptake. These methionine probably coordinate copper during the process of metal transport.


:

Pssm-ID: 461194  Cd Length: 151  Bit Score: 98.15  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  290 MYFHFGYSDY-ILFDSWVPRSTFSYALGCLFCFLLAIGYEFLLVVGSGLDTAWKMVESSRhsndvglgdtlelpmsgsdh 368
Cdd:pfam04145   1 MLFNWSTIDTcLLFKSWHITSTGAFAGSCIGLFLLAVLYEFLRALRARLERRYDRWLARR-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  369 sfglyrspmenpnisvlsddtpllrprsritgkrrtslnisthpklqpnhesqnlplcpttdltdqidmgpdgeeesvfd 448
Cdd:pfam04145     --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  449 hsmsessshiHQRVISHGNTSQAAGLSDFLQHHSGDISHHSNQHTPTQylsrlyTKKWTHLQMRIGRALIRLVTITLAYI 528
Cdd:pfam04145  61 ----------ARARSRSVSAASSSSSASSSSGDSSASESVPVLLRSGF------SPRPFRPSVDLIRALLHAVQVGLGYL 124
                         250       260
                  ....*....|....*....|....*.
gi 328774125  529 CMLLVMSFNVGLFLSVVVGLAVGKFM 554
Cdd:pfam04145 125 LMLAVMTYNGYYFLAVVLGAFLGYFL 150
 
Name Accession Description Interval E-value
Ctr pfam04145
Ctr copper transporter family; The redox active metal copper is an essential cofactor in ...
290-554 4.89e-24

Ctr copper transporter family; The redox active metal copper is an essential cofactor in critical biological processes such as respiration, iron transport, oxidative stress protection, hormone production, and pigmentation. A widely conserved family of high-affinity copper transport proteins (Ctr proteins) mediates copper uptake at the plasma membrane. A series of clustered methionine residues in the hydrophilic extracellular domain, and an MXXXM motif in the second transmembrane domain, are important for copper uptake. These methionine probably coordinate copper during the process of metal transport.


Pssm-ID: 461194  Cd Length: 151  Bit Score: 98.15  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  290 MYFHFGYSDY-ILFDSWVPRSTFSYALGCLFCFLLAIGYEFLLVVGSGLDTAWKMVESSRhsndvglgdtlelpmsgsdh 368
Cdd:pfam04145   1 MLFNWSTIDTcLLFKSWHITSTGAFAGSCIGLFLLAVLYEFLRALRARLERRYDRWLARR-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  369 sfglyrspmenpnisvlsddtpllrprsritgkrrtslnisthpklqpnhesqnlplcpttdltdqidmgpdgeeesvfd 448
Cdd:pfam04145     --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  449 hsmsessshiHQRVISHGNTSQAAGLSDFLQHHSGDISHHSNQHTPTQylsrlyTKKWTHLQMRIGRALIRLVTITLAYI 528
Cdd:pfam04145  61 ----------ARARSRSVSAASSSSSASSSSGDSSASESVPVLLRSGF------SPRPFRPSVDLIRALLHAVQVGLGYL 124
                         250       260
                  ....*....|....*....|....*.
gi 328774125  529 CMLLVMSFNVGLFLSVVVGLAVGKFM 554
Cdd:pfam04145 125 LMLAVMTYNGYYFLAVVLGAFLGYFL 150
 
Name Accession Description Interval E-value
Ctr pfam04145
Ctr copper transporter family; The redox active metal copper is an essential cofactor in ...
290-554 4.89e-24

Ctr copper transporter family; The redox active metal copper is an essential cofactor in critical biological processes such as respiration, iron transport, oxidative stress protection, hormone production, and pigmentation. A widely conserved family of high-affinity copper transport proteins (Ctr proteins) mediates copper uptake at the plasma membrane. A series of clustered methionine residues in the hydrophilic extracellular domain, and an MXXXM motif in the second transmembrane domain, are important for copper uptake. These methionine probably coordinate copper during the process of metal transport.


Pssm-ID: 461194  Cd Length: 151  Bit Score: 98.15  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  290 MYFHFGYSDY-ILFDSWVPRSTFSYALGCLFCFLLAIGYEFLLVVGSGLDTAWKMVESSRhsndvglgdtlelpmsgsdh 368
Cdd:pfam04145   1 MLFNWSTIDTcLLFKSWHITSTGAFAGSCIGLFLLAVLYEFLRALRARLERRYDRWLARR-------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  369 sfglyrspmenpnisvlsddtpllrprsritgkrrtslnisthpklqpnhesqnlplcpttdltdqidmgpdgeeesvfd 448
Cdd:pfam04145     --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328774125  449 hsmsessshiHQRVISHGNTSQAAGLSDFLQHHSGDISHHSNQHTPTQylsrlyTKKWTHLQMRIGRALIRLVTITLAYI 528
Cdd:pfam04145  61 ----------ARARSRSVSAASSSSSASSSSGDSSASESVPVLLRSGF------SPRPFRPSVDLIRALLHAVQVGLGYL 124
                         250       260
                  ....*....|....*....|....*.
gi 328774125  529 CMLLVMSFNVGLFLSVVVGLAVGKFM 554
Cdd:pfam04145 125 LMLAVMTYNGYYFLAVVLGAFLGYFL 150
 
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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