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Conserved domains on  [gi|1972267507|ref|NP_001379479|]
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Protein disulfide isomerase crld-1 [Caenorhabditis elegans]

Protein Classification

DUF3456 and EGF_CA domain-containing protein( domain architecture ID 10320464)

DUF3456 and EGF_CA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3456 super family cl13389
TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, ...
 26-135 4.77e-10

TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, is PRAT4 (A and B), a Protein Associated with Toll-like receptor 4. The Toll family of receptors - TLRs - plays an essential role in innate recognition of microbial products, the first line of defence against bacterial infection. PRAT4A influences the subcellular distribution and the strength of TLR responses and alters the relative activity of each TLR. PRAT4B regulates TLR4 trafficking to the cell surface and the extent of its expression there. TLR4 recognizes lipopolysaccharide (LPS), one of the most immuno-stimulatory glycolipids constituting the outer membrane of the Gram-negative bacteria. This family has also been described as a SAP-like MIR-interacting protein family.


The actual alignment was detected with superfamily member pfam11938:

Pssm-ID: 463404  Cd Length: 151  Bit Score: 56.95  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267507  26 KCRTCNFLVSTFDEGLKKTARHH------FAGGDTAWEEKNLGKYKTSETRLIEVLEGVC-----------KKSSLPNMD 88
Cdd:pfam11938   1 KCEVCKALADELEYALSKTDPSKevdvggFRLDPDGKRKKKKIPYARSELRLTELLEGVCermldynlhkeRSTSTRTFV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972267507  89 NFMG-----------------------IAEIEFKCSTQLEKHEETIEEFYYN-QQHNNMSNWLCVEQLKLC 135
Cdd:pfam11938  81 TLHGlnkgvkvdlgipyelwdepsaevNKSLKFQCETIVEEYEDEIEEWYFNhQDEKDLEKYLCSEDSDLC 151
EGF_CA smart00179
Calcium-binding EGF-like domain;
241-282 5.50e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972267507  241 DVNECQNESACtKEHEICVNTVGSFKCECKEGYKkdDEQNCQ 282
Cdd:smart00179   1 DIDECASGNPC-QNGGTCVNTVGSYRCECPPGYT--DGRNCE 39
 
Name Accession Description Interval E-value
DUF3456 pfam11938
TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, ...
 26-135 4.77e-10

TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, is PRAT4 (A and B), a Protein Associated with Toll-like receptor 4. The Toll family of receptors - TLRs - plays an essential role in innate recognition of microbial products, the first line of defence against bacterial infection. PRAT4A influences the subcellular distribution and the strength of TLR responses and alters the relative activity of each TLR. PRAT4B regulates TLR4 trafficking to the cell surface and the extent of its expression there. TLR4 recognizes lipopolysaccharide (LPS), one of the most immuno-stimulatory glycolipids constituting the outer membrane of the Gram-negative bacteria. This family has also been described as a SAP-like MIR-interacting protein family.


Pssm-ID: 463404  Cd Length: 151  Bit Score: 56.95  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267507  26 KCRTCNFLVSTFDEGLKKTARHH------FAGGDTAWEEKNLGKYKTSETRLIEVLEGVC-----------KKSSLPNMD 88
Cdd:pfam11938   1 KCEVCKALADELEYALSKTDPSKevdvggFRLDPDGKRKKKKIPYARSELRLTELLEGVCermldynlhkeRSTSTRTFV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972267507  89 NFMG-----------------------IAEIEFKCSTQLEKHEETIEEFYYN-QQHNNMSNWLCVEQLKLC 135
Cdd:pfam11938  81 TLHGlnkgvkvdlgipyelwdepsaevNKSLKFQCETIVEEYEDEIEEWYFNhQDEKDLEKYLCSEDSDLC 151
EGF_CA smart00179
Calcium-binding EGF-like domain;
241-282 5.50e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972267507  241 DVNECQNESACtKEHEICVNTVGSFKCECKEGYKkdDEQNCQ 282
Cdd:smart00179   1 DIDECASGNPC-QNGGTCVNTVGSYRCECPPGYT--DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 241-273 2.35e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.70  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972267507 241 DVNECQNESACtKEHEICVNTVGSFKCECKEGY 273
Cdd:cd00054     1 DIDECASGNPC-QNGGTCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
241-272 2.20e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.99  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972267507 241 DVNECQNESACTKEHEICVNTVGSFKCECKEG 272
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
 
Name Accession Description Interval E-value
DUF3456 pfam11938
TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, ...
 26-135 4.77e-10

TLR4 regulator and MIR-interacting MSAP; This family of proteins, found from plants to humans, is PRAT4 (A and B), a Protein Associated with Toll-like receptor 4. The Toll family of receptors - TLRs - plays an essential role in innate recognition of microbial products, the first line of defence against bacterial infection. PRAT4A influences the subcellular distribution and the strength of TLR responses and alters the relative activity of each TLR. PRAT4B regulates TLR4 trafficking to the cell surface and the extent of its expression there. TLR4 recognizes lipopolysaccharide (LPS), one of the most immuno-stimulatory glycolipids constituting the outer membrane of the Gram-negative bacteria. This family has also been described as a SAP-like MIR-interacting protein family.


Pssm-ID: 463404  Cd Length: 151  Bit Score: 56.95  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267507  26 KCRTCNFLVSTFDEGLKKTARHH------FAGGDTAWEEKNLGKYKTSETRLIEVLEGVC-----------KKSSLPNMD 88
Cdd:pfam11938   1 KCEVCKALADELEYALSKTDPSKevdvggFRLDPDGKRKKKKIPYARSELRLTELLEGVCermldynlhkeRSTSTRTFV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972267507  89 NFMG-----------------------IAEIEFKCSTQLEKHEETIEEFYYN-QQHNNMSNWLCVEQLKLC 135
Cdd:pfam11938  81 TLHGlnkgvkvdlgipyelwdepsaevNKSLKFQCETIVEEYEDEIEEWYFNhQDEKDLEKYLCSEDSDLC 151
EGF_CA smart00179
Calcium-binding EGF-like domain;
241-282 5.50e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 5.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972267507  241 DVNECQNESACtKEHEICVNTVGSFKCECKEGYKkdDEQNCQ 282
Cdd:smart00179   1 DIDECASGNPC-QNGGTCVNTVGSYRCECPPGYT--DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 241-273 2.35e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.70  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972267507 241 DVNECQNESACtKEHEICVNTVGSFKCECKEGY 273
Cdd:cd00054     1 DIDECASGNPC-QNGGTCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
241-272 2.20e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.99  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972267507 241 DVNECQNESACTKEHEICVNTVGSFKCECKEG 272
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
 
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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