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Conserved domains on  [gi|1270475058|gb|PHS66668.1|]
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hypothetical protein COB09_03835 [Thalassobium sp.]

Protein Classification

heavy metal translocating P-type ATPase( domain architecture ID 10007244)

heavy metal translocating P-type ATPase such as copper-translocating P-type ATPase that couples the hydrolysis of ATP with the export of Cu(+) or Cu(2+); P-type ATPases are distinguished from other transport ATPases (F-, V-, and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YHS COG3350
Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport ...
 12-37 5.49e-07

Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism];


:

Pssm-ID: 442578  Cd Length: 56  Bit Score: 44.31  E-value: 5.49e-07
                          10        20
                  ....*....|....*....|....*.
gi 1270475058  12 YRGIDHYFCSSQCLDRFKAHPHLFVG 37
Cdd:COG3350    27 YDGKTYYFCSEECRDKFKANPEKYLP 52
 
Name Accession Description Interval E-value
YHS COG3350
Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport ...
 12-37 5.49e-07

Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism];


Pssm-ID: 442578  Cd Length: 56  Bit Score: 44.31  E-value: 5.49e-07
                          10        20
                  ....*....|....*....|....*.
gi 1270475058  12 YRGIDHYFCSSQCLDRFKAHPHLFVG 37
Cdd:COG3350    27 YDGKTYYFCSEECRDKFKANPEKYLP 52
YHS pfam04945
YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains ...
 12-37 2.86e-03

YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterized membrane proteins including Swiss:Q9CNI0. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.


Pssm-ID: 461496 [Multi-domain]  Cd Length: 46  Bit Score: 33.88  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*.
gi 1270475058  12 YRGIDHYFCSSQCLDRFKAHPHLFVG 37
Cdd:pfam04945  19 YKGKEYYFCSEGCLDIFDDDPEKYAG 44
TRASH smart00746
metallochaperone-like domain;
5-32 6.81e-03

metallochaperone-like domain;


Pssm-ID: 214799  Cd Length: 39  Bit Score: 32.73  E-value: 6.81e-03
                           10        20
                   ....*....|....*....|....*...
gi 1270475058    5 DRSLLFNYRGIDHYFCSSQCLDRFKAHP 32
Cdd:smart00746  12 GTGIMVVNDGKVYYFCSSKCLSKFKKKR 39
 
Name Accession Description Interval E-value
YHS COG3350
Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport ...
 12-37 5.49e-07

Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism];


Pssm-ID: 442578  Cd Length: 56  Bit Score: 44.31  E-value: 5.49e-07
                          10        20
                  ....*....|....*....|....*.
gi 1270475058  12 YRGIDHYFCSSQCLDRFKAHPHLFVG 37
Cdd:COG3350    27 YDGKTYYFCSEECRDKFKANPEKYLP 52
YHS pfam04945
YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains ...
 12-37 2.86e-03

YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterized membrane proteins including Swiss:Q9CNI0. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.


Pssm-ID: 461496 [Multi-domain]  Cd Length: 46  Bit Score: 33.88  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*.
gi 1270475058  12 YRGIDHYFCSSQCLDRFKAHPHLFVG 37
Cdd:pfam04945  19 YKGKEYYFCSEGCLDIFDDDPEKYAG 44
TRASH smart00746
metallochaperone-like domain;
5-32 6.81e-03

metallochaperone-like domain;


Pssm-ID: 214799  Cd Length: 39  Bit Score: 32.73  E-value: 6.81e-03
                           10        20
                   ....*....|....*....|....*...
gi 1270475058    5 DRSLLFNYRGIDHYFCSSQCLDRFKAHP 32
Cdd:smart00746  12 GTGIMVVNDGKVYYFCSSKCLSKFKKKR 39
 
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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