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Conserved domains on  [gi|970841892|ref|NP_001305150|]
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alpha-hemoglobin-stabilizing protein [Homo sapiens]

Protein Classification

AHSP domain-containing protein( domain architecture ID 10557926)

AHSP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AHSP pfam09236
Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a ...
5-91 7.42e-59

Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a molecular chaperone for free alpha-haemoglobin, preventing the harmful aggregation of alpha-haemoglobin during normal erythroid cell development: it specifically protects free alpha-haemoglobin from precipitation. AHSP adopts a helical secondary structure consisting of an elongated antiparallel three alpha-helix bundle.


:

Pssm-ID: 462718  Cd Length: 87  Bit Score: 175.31  E-value: 7.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970841892    5 KANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAK 84
Cdd:pfam09236   1 QANKDLISSGMKEFNVLLNQQVFSDPLISEEAMVTVVNDWVNFYINYYRQQMTGEQQEQDRALQELRQELNTLASPFLAK 80

                  ....*..
gi 970841892   85 YRDFLKS 91
Cdd:pfam09236  81 YRAFLKS 87
 
Name Accession Description Interval E-value
AHSP pfam09236
Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a ...
5-91 7.42e-59

Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a molecular chaperone for free alpha-haemoglobin, preventing the harmful aggregation of alpha-haemoglobin during normal erythroid cell development: it specifically protects free alpha-haemoglobin from precipitation. AHSP adopts a helical secondary structure consisting of an elongated antiparallel three alpha-helix bundle.


Pssm-ID: 462718  Cd Length: 87  Bit Score: 175.31  E-value: 7.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970841892    5 KANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAK 84
Cdd:pfam09236   1 QANKDLISSGMKEFNVLLNQQVFSDPLISEEAMVTVVNDWVNFYINYYRQQMTGEQQEQDRALQELRQELNTLASPFLAK 80

                  ....*..
gi 970841892   85 YRDFLKS 91
Cdd:pfam09236  81 YRAFLKS 87
 
Name Accession Description Interval E-value
AHSP pfam09236
Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a ...
5-91 7.42e-59

Alpha-haemoglobin stabilising protein; Alpha-haemoglobin stabilising protein (AHSP) acts a molecular chaperone for free alpha-haemoglobin, preventing the harmful aggregation of alpha-haemoglobin during normal erythroid cell development: it specifically protects free alpha-haemoglobin from precipitation. AHSP adopts a helical secondary structure consisting of an elongated antiparallel three alpha-helix bundle.


Pssm-ID: 462718  Cd Length: 87  Bit Score: 175.31  E-value: 7.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970841892    5 KANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAK 84
Cdd:pfam09236   1 QANKDLISSGMKEFNVLLNQQVFSDPLISEEAMVTVVNDWVNFYINYYRQQMTGEQQEQDRALQELRQELNTLASPFLAK 80

                  ....*..
gi 970841892   85 YRDFLKS 91
Cdd:pfam09236  81 YRAFLKS 87
 
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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