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Conserved domains on  [gi|189082685|sp|A2RUU4|]
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RecName: Full=Colipase-like protein 1; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLIPASE super family cl29842
Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor ...
 23-110 1.38e-37

Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor itself to the water-lipid interface and stabilizing the active enzyme conformation


The actual alignment was detected with superfamily member cd00039:

Pssm-ID: 475263  Cd Length: 90  Bit Score: 122.24  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189082685  23 GSLSPTKYNLLELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSK--NEKWL 100
Cdd:cd00039    1 APDPRGIIINLEAGELCLNSAQCKSGCCQHASSLSLARCAAKASENSECSPQTLYGVYYKCPCERGLTCEGDKsiVGSIT 80

                         90
                 ....*....|
gi 189082685 101 SIAYGRCQKI 110
Cdd:cd00039   81 NTNYGICLDA 90
 
Name Accession Description Interval E-value
COLIPASE cd00039
Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor ...
 23-110 1.38e-37

Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor itself to the water-lipid interface and stabilizing the active enzyme conformation


Pssm-ID: 119409  Cd Length: 90  Bit Score: 122.24  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189082685  23 GSLSPTKYNLLELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSK--NEKWL 100
Cdd:cd00039    1 APDPRGIIINLEAGELCLNSAQCKSGCCQHASSLSLARCAAKASENSECSPQTLYGVYYKCPCERGLTCEGDKsiVGSIT 80

                         90
                 ....*....|
gi 189082685 101 SIAYGRCQKI 110
Cdd:cd00039   81 NTNYGICLDA 90
COLIPASE smart00023
Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which ...
 33-114 1.16e-09

Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.


Pssm-ID: 128339  Cd Length: 95  Bit Score: 51.37  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189082685    33 LELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSKN--EKWLSIAYGRCQKI 110
Cdd:smart00023  11 LEAGELCLNSAQCKSGCCQHDSGLSLARCAPKASENSECSAKTLYGVYYKCPCERGLTCEGDKSivGSITNTNFGICHDA 90


                   ....
gi 189082685   111 GRQK 114
Cdd:smart00023  91 GRSK 94
 
Name Accession Description Interval E-value
COLIPASE cd00039
Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor ...
 23-110 1.38e-37

Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor itself to the water-lipid interface and stabilizing the active enzyme conformation


Pssm-ID: 119409  Cd Length: 90  Bit Score: 122.24  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189082685  23 GSLSPTKYNLLELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSK--NEKWL 100
Cdd:cd00039    1 APDPRGIIINLEAGELCLNSAQCKSGCCQHASSLSLARCAAKASENSECSPQTLYGVYYKCPCERGLTCEGDKsiVGSIT 80

                         90
                 ....*....|
gi 189082685 101 SIAYGRCQKI 110
Cdd:cd00039   81 NTNYGICLDA 90
COLIPASE smart00023
Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which ...
 33-114 1.16e-09

Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.


Pssm-ID: 128339  Cd Length: 95  Bit Score: 51.37  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189082685    33 LELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSKN--EKWLSIAYGRCQKI 110
Cdd:smart00023  11 LEAGELCLNSAQCKSGCCQHDSGLSLARCAPKASENSECSAKTLYGVYYKCPCERGLTCEGDKSivGSITNTNFGICHDA 90


                   ....
gi 189082685   111 GRQK 114
Cdd:smart00023  91 GRSK 94
CLPS cd23011
Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme ...
 33-91 3.21e-07

Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. Bile salts, at concentrations near their critical micellar concentration, desorb lipase from emulsified triacylglycerol and, thereby, inhibit lipolysis. Colipase functions by anchoring pancreatic lipase to the lipid-water interface through the formation of the stoichiometric colipase-lipase complex.


Pssm-ID: 437996  Cd Length: 84  Bit Score: 44.58  E-value: 3.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189082685  33 LELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTC 91
Cdd:cd23011    6 LDNGELCLNSAQCKSGCCHRDSGLSLARCAPKAAENQECSPKTLYGVYYKCPCESGLTC 64
 
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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