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Conserved domains on  [gi|4929893]
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Protein Classification

Antifreeze_III domain-containing protein (domain architecture ID 10184334)

Antifreeze_III domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Antifreeze_III cd11617
Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III ...
4-65 5.24e-30

Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III inhibits the growth of ice crystals and protects fish from cold damage in sub-freezing temperatures.


:

Pssm-ID: 212162  Cd Length: 62  Bit Score: 99.85  E-value: 5.24e-30
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4929893   4 ASVVANQLIPINTALTLAMMRSEVVTPVGIPAEDIPRLVSMQVNRAVPLGTTLMPDMVKGYA 65
Cdd:cd11617  1 ASVVATQLIPINTALTLVMMKAKVVTPMGIPAEEIPRLVGMQVNRAVPLGTTLMPDMVKGYA 62
 
Name Accession Description Interval E-value
Antifreeze_III cd11617
Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III ...
4-65 5.24e-30

Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III inhibits the growth of ice crystals and protects fish from cold damage in sub-freezing temperatures.


Pssm-ID: 212162  Cd Length: 62  Bit Score: 99.85  E-value: 5.24e-30
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4929893   4 ASVVANQLIPINTALTLAMMRSEVVTPVGIPAEDIPRLVSMQVNRAVPLGTTLMPDMVKGYA 65
Cdd:cd11617  1 ASVVATQLIPINTALTLVMMKAKVVTPMGIPAEEIPRLVGMQVNRAVPLGTTLMPDMVKGYA 62
 
Name Accession Description Interval E-value
Antifreeze_III cd11617
Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III ...
4-65 5.24e-30

Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III inhibits the growth of ice crystals and protects fish from cold damage in sub-freezing temperatures.


Pssm-ID: 212162  Cd Length: 62  Bit Score: 99.85  E-value: 5.24e-30
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4929893   4 ASVVANQLIPINTALTLAMMRSEVVTPVGIPAEDIPRLVSMQVNRAVPLGTTLMPDMVKGYA 65
Cdd:cd11617  1 ASVVATQLIPINTALTLVMMKAKVVTPMGIPAEEIPRLVGMQVNRAVPLGTTLMPDMVKGYA 62
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
5-61 2.74e-05

C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).


Pssm-ID: 212160 [Multi-domain]  Cd Length: 58  Bit Score: 36.93  E-value: 2.74e-05
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....*..
gi 4929893   5 SVVANQLIPINTALTLAMMRSeVVTPVGIPAEDIPRLVSMQVNRAVPLGTTLMPDMV 61
Cdd:cd11615  3 SLVAARDIKAGEVLTEENLRV-KRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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