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Conserved domains on  [gi|1907167177|ref|XP_036021494|]
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LIM and calponin homology domains-containing protein 1 isoform X2 [Mus musculus]

Protein Classification

DUF4757 domain-containing protein( domain architecture ID 11067598)

DUF4757 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 580-713 6.11e-40

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


:

Pssm-ID: 464950  Cd Length: 170  Bit Score: 145.66  E-value: 6.11e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907167177  580 REQNEEVIQKEHEMLPRVQRPE-ECSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDDK 658
Cdd:pfam15949   39 RAEKEEDIRRSWSTRTQPSKVAyPPRQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEEDK 116

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907167177  659 WQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 713
Cdd:pfam15949  117 WQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
DUF4757 super family cl24502
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 91-152 3.45e-19

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


The actual alignment was detected with superfamily member pfam15949:

Pssm-ID: 464950  Cd Length: 170  Bit Score: 86.34  E-value: 3.45e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907167177   91 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEF-RKSWSTATSPLGGERPF 152
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1066-1103 8.99e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907167177 1066 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1103
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
Name Accession Description Interval E-value
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 580-713 6.11e-40

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 464950  Cd Length: 170  Bit Score: 145.66  E-value: 6.11e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907167177  580 REQNEEVIQKEHEMLPRVQRPE-ECSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDDK 658
Cdd:pfam15949   39 RAEKEEDIRRSWSTRTQPSKVAyPPRQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEEDK 116

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907167177  659 WQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 713
Cdd:pfam15949  117 WQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 91-152 3.45e-19

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 464950  Cd Length: 170  Bit Score: 86.34  E-value: 3.45e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907167177   91 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEF-RKSWSTATSPLGGERPF 152
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1066-1103 8.99e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907167177 1066 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1103
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
Name Accession Description Interval E-value
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 580-713 6.11e-40

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 464950  Cd Length: 170  Bit Score: 145.66  E-value: 6.11e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907167177  580 REQNEEVIQKEHEMLPRVQRPE-ECSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDDK 658
Cdd:pfam15949   39 RAEKEEDIRRSWSTRTQPSKVAyPPRQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEEDK 116

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907167177  659 WQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 713
Cdd:pfam15949  117 WQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 91-152 3.45e-19

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 464950  Cd Length: 170  Bit Score: 86.34  E-value: 3.45e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907167177   91 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEF-RKSWSTATSPLGGERPF 152
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1066-1103 8.99e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907167177 1066 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1103
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
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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