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Conserved domains on  [gi|1084307475|ref|XP_018645336|]
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12.5 kDa retinal tissue protein (Rtp12.5),putative [Schistosoma mansoni]

Protein Classification

LIN52 domain-containing protein( domain architecture ID 10562158)

LIN52 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
9-103 1.31e-48

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


:

Pssm-ID: 462950  Cd Length: 92  Bit Score: 149.69  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084307475   9 LLSHDNLDRASPDLWPEQIPGVTEFLTsrqNEINLHTPPKYATDLDKEDLELIHDFGSLSTQQLMDKIKHLQNLAYQVGL 88
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLT---MSSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGL 77
                          90
                  ....*....|....*
gi 1084307475  89 EEAKEMTRGKFLNIL 103
Cdd:pfam10044  78 EEAKEMTRGKLLNIF 92
 
Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
9-103 1.31e-48

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


Pssm-ID: 462950  Cd Length: 92  Bit Score: 149.69  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084307475   9 LLSHDNLDRASPDLWPEQIPGVTEFLTsrqNEINLHTPPKYATDLDKEDLELIHDFGSLSTQQLMDKIKHLQNLAYQVGL 88
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLT---MSSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGL 77
                          90
                  ....*....|....*
gi 1084307475  89 EEAKEMTRGKFLNIL 103
Cdd:pfam10044  78 EEAKEMTRGKLLNIF 92
 
Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
9-103 1.31e-48

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


Pssm-ID: 462950  Cd Length: 92  Bit Score: 149.69  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084307475   9 LLSHDNLDRASPDLWPEQIPGVTEFLTsrqNEINLHTPPKYATDLDKEDLELIHDFGSLSTQQLMDKIKHLQNLAYQVGL 88
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLT---MSSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGL 77
                          90
                  ....*....|....*
gi 1084307475  89 EEAKEMTRGKFLNIL 103
Cdd:pfam10044  78 EEAKEMTRGKLLNIF 92
 
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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