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Conserved domains on  [gi|1039752611|ref|XP_017172711|]
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demilune cell and parotid protein isoform X1 [Mus musculus]

Protein Classification

jacalin family lectin( domain architecture ID 5034)

jacalin family lectin is a sugar-binding protein containing a jacalin domain

Gene Ontology:  GO:0030246
PubMed:  28737678|15329359

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jacalin_like super family cl03205
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 53-183 6.37e-25

Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.


The actual alignment was detected with superfamily member cd09611:

Pssm-ID: 446042 [Multi-domain]  Cd Length: 128  Bit Score: 93.93  E-value: 6.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752611  53 GPEVGKHSCTSAPEGKNITSIRVFLKGRLIVGIQLNYDDNKDgQVYGSTAGKEMVARLSKEEHIIAAQGTYTPsALTQII 132
Cdd:cd09611     1 GSGGGKYFSDVGEGGGPITGIRVSVGNNYIKGIQVRYGSNWS-DVYGGRGGNEQEIVLEPGESITKVSGSYKI-YLHGLV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039752611 133 FTTNQPRQLMVGYYVGNSeYSSFPNDPSHVLKGACVSWRAGGIKSILFLWG 183
Cdd:cd09611    79 FTTNKGRYLSFGKLRGRS-FNATPPPSNYVLRGISGRYGGLGIKSIGFHWG 128
 
Name Accession Description Interval E-value
Jacalin_ZG16_like cd09611
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ...
 53-183 6.37e-25

Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.


Pssm-ID: 187707 [Multi-domain]  Cd Length: 128  Bit Score: 93.93  E-value: 6.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752611  53 GPEVGKHSCTSAPEGKNITSIRVFLKGRLIVGIQLNYDDNKDgQVYGSTAGKEMVARLSKEEHIIAAQGTYTPsALTQII 132
Cdd:cd09611     1 GSGGGKYFSDVGEGGGPITGIRVSVGNNYIKGIQVRYGSNWS-DVYGGRGGNEQEIVLEPGESITKVSGSYKI-YLHGLV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039752611 133 FTTNQPRQLMVGYYVGNSeYSSFPNDPSHVLKGACVSWRAGGIKSILFLWG 183
Cdd:cd09611    79 FTTNKGRYLSFGKLRGRS-FNATPPPSNYVLRGISGRYGGLGIKSIGFHWG 128
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 69-165 3.98e-09

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 52.62  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752611   69 NITSIRVFLKGRLIVGIQLNYDDNKD--GQVYGSTAGKEMVARLSKEEHIIAAQGTYTPSA-LTQIIFTTNQPRQLMVGY 145
Cdd:smart00915  11 GVRKIYVGQGGEGIKSIQFDYDKGGKvwGDEHGGKGGTGEEILLYPGEYITSVEGTYDKSGvITSLTFKTNKGRTSPFGG 90

                           90       100
                   ....*....|....*....|
gi 1039752611  146 YVGNSEYsSFPNDPSHVLKG 165
Cdd:smart00915  91 YEGGTKF-VLESKEGKKIVG 109
 
Name Accession Description Interval E-value
Jacalin_ZG16_like cd09611
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ...
 53-183 6.37e-25

Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.


Pssm-ID: 187707 [Multi-domain]  Cd Length: 128  Bit Score: 93.93  E-value: 6.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752611  53 GPEVGKHSCTSAPEGKNITSIRVFLKGRLIVGIQLNYDDNKDgQVYGSTAGKEMVARLSKEEHIIAAQGTYTPsALTQII 132
Cdd:cd09611     1 GSGGGKYFSDVGEGGGPITGIRVSVGNNYIKGIQVRYGSNWS-DVYGGRGGNEQEIVLEPGESITKVSGSYKI-YLHGLV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039752611 133 FTTNQPRQLMVGYYVGNSeYSSFPNDPSHVLKGACVSWRAGGIKSILFLWG 183
Cdd:cd09611    79 FTTNKGRYLSFGKLRGRS-FNATPPPSNYVLRGISGRYGGLGIKSIGFHWG 128
Jacalin smart00915
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ...
 69-165 3.98e-09

Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.


Pssm-ID: 214909 [Multi-domain]  Cd Length: 128  Bit Score: 52.62  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752611   69 NITSIRVFLKGRLIVGIQLNYDDNKD--GQVYGSTAGKEMVARLSKEEHIIAAQGTYTPSA-LTQIIFTTNQPRQLMVGY 145
Cdd:smart00915  11 GVRKIYVGQGGEGIKSIQFDYDKGGKvwGDEHGGKGGTGEEILLYPGEYITSVEGTYDKSGvITSLTFKTNKGRTSPFGG 90

                           90       100
                   ....*....|....*....|
gi 1039752611  146 YVGNSEYsSFPNDPSHVLKG 165
Cdd:smart00915  91 YEGGTKF-VLESKEGKKIVG 109
 
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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