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Conserved domains on  [gi|116242801|sp|P37108|]
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RecName: Full=Signal recognition particle 14 kDa protein; Short=SRP14; AltName: Full=18 kDa Alu RNA-binding protein

Protein Classification

signal recognition particle 14 kDa protein( domain architecture ID 10491636)

signal recognition particle 14 kDa protein (SRP14) is a component of the signal-recognition-particle (SRP) assembly that has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane

CATH:  3.30.720.10
Gene Ontology:  GO:0008312|GO:0030942|GO:0006614|GO:0005786
PubMed:  17507650|12605305

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRP14 pfam02290
Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a ...
 4-94 6.83e-31

Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a multimeric protein involved in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP14 and SRP9 form a complex essential for SRP RNA binding.


:

Pssm-ID: 460524  Cd Length: 106  Bit Score: 106.25  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242801    4 LESEQFLTELTRLFQKCRTS--GSVYITLKK--YDGRTKPIPKKGTVEGF----------EPADNKCLLRATDGK-KKIS 68
Cdd:pfam02290   1 LSNDEFLTELTELFEKAKEKghGSVYLTQKRltYDDRVKPRYDKSKPSKStadpepdlapSDKEYPCLIRATDGKkKKIS 80

                          90       100
                  ....*....|....*....|....*.
gi 116242801   69 TVVSSKEVNKFQMAYSNLLRANMDGL 94
Cdd:pfam02290  81 TVVEPDDLDKFWARYAEVLKAGMDGL 106
 
Name Accession Description Interval E-value
SRP14 pfam02290
Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a ...
 4-94 6.83e-31

Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a multimeric protein involved in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP14 and SRP9 form a complex essential for SRP RNA binding.


Pssm-ID: 460524  Cd Length: 106  Bit Score: 106.25  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242801    4 LESEQFLTELTRLFQKCRTS--GSVYITLKK--YDGRTKPIPKKGTVEGF----------EPADNKCLLRATDGK-KKIS 68
Cdd:pfam02290   1 LSNDEFLTELTELFEKAKEKghGSVYLTQKRltYDDRVKPRYDKSKPSKStadpepdlapSDKEYPCLIRATDGKkKKIS 80

                          90       100
                  ....*....|....*....|....*.
gi 116242801   69 TVVSSKEVNKFQMAYSNLLRANMDGL 94
Cdd:pfam02290  81 TVVEPDDLDKFWARYAEVLKAGMDGL 106
 
Name Accession Description Interval E-value
SRP14 pfam02290
Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a ...
 4-94 6.83e-31

Signal recognition particle 14kD protein; The signal recognition particle (SRP) is a multimeric protein involved in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP14 and SRP9 form a complex essential for SRP RNA binding.


Pssm-ID: 460524  Cd Length: 106  Bit Score: 106.25  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242801    4 LESEQFLTELTRLFQKCRTS--GSVYITLKK--YDGRTKPIPKKGTVEGF----------EPADNKCLLRATDGK-KKIS 68
Cdd:pfam02290   1 LSNDEFLTELTELFEKAKEKghGSVYLTQKRltYDDRVKPRYDKSKPSKStadpepdlapSDKEYPCLIRATDGKkKKIS 80

                          90       100
                  ....*....|....*....|....*.
gi 116242801   69 TVVSSKEVNKFQMAYSNLLRANMDGL 94
Cdd:pfam02290  81 TVVEPDDLDKFWARYAEVLKAGMDGL 106
 
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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