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Conserved domains on  [gi|665400307|ref|NP_001097280|]
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uncharacterized protein Dmel_CG34231 [Drosophila melanogaster]

Protein Classification

RNA-binding protein( domain architecture ID 106745)

RNA-binding protein containing an RNA recognition motif (RRM)

CATH:  3.30.70.330
Gene Ontology:  GO:0003723
PubMed:  15853797
SCOP:  3000110

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
30-122 2.34e-42

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member cd12442:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 100  Bit Score: 136.57  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400307  30 VKVYTVASESRHLLIFGVPKINLQANLRTKLQGFGKVQSCISVTSEMAskmdlEAFTDVFAVKFERLEVARRAKKMLDAH 109
Cdd:cd12442    1 VKVYTVNQESRYLLVQGVPALGVEEELLKLFSLYGTIEEYRILDEYPC-----EEFTEVYLIKFERIQSARFAKRKLDDH 75
                         90
                 ....*....|...
gi 665400307 110 QFYGGILHISYAP 122
Cdd:cd12442   76 SFFGGILHVCYAP 88
 
Name Accession Description Interval E-value
RRM_RBM48 cd12442
RNA recognition motif (RRM) found in RNA-binding protein 48 (RBM48) and similar proteins; This ...
30-122 2.34e-42

RNA recognition motif (RRM) found in RNA-binding protein 48 (RBM48) and similar proteins; This subfamily corresponds to the RRM of RBM48, a putative RNA-binding protein of unknown function. It contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409876 [Multi-domain]  Cd Length: 100  Bit Score: 136.57  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400307  30 VKVYTVASESRHLLIFGVPKINLQANLRTKLQGFGKVQSCISVTSEMAskmdlEAFTDVFAVKFERLEVARRAKKMLDAH 109
Cdd:cd12442    1 VKVYTVNQESRYLLVQGVPALGVEEELLKLFSLYGTIEEYRILDEYPC-----EEFTEVYLIKFERIQSARFAKRKLDDH 75
                         90
                 ....*....|...
gi 665400307 110 QFYGGILHISYAP 122
Cdd:cd12442   76 SFFGGILHVCYAP 88
 
Name Accession Description Interval E-value
RRM_RBM48 cd12442
RNA recognition motif (RRM) found in RNA-binding protein 48 (RBM48) and similar proteins; This ...
30-122 2.34e-42

RNA recognition motif (RRM) found in RNA-binding protein 48 (RBM48) and similar proteins; This subfamily corresponds to the RRM of RBM48, a putative RNA-binding protein of unknown function. It contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409876 [Multi-domain]  Cd Length: 100  Bit Score: 136.57  E-value: 2.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400307  30 VKVYTVASESRHLLIFGVPKINLQANLRTKLQGFGKVQSCISVTSEMAskmdlEAFTDVFAVKFERLEVARRAKKMLDAH 109
Cdd:cd12442    1 VKVYTVNQESRYLLVQGVPALGVEEELLKLFSLYGTIEEYRILDEYPC-----EEFTEVYLIKFERIQSARFAKRKLDDH 75
                         90
                 ....*....|...
gi 665400307 110 QFYGGILHISYAP 122
Cdd:cd12442   76 SFFGGILHVCYAP 88
RRM1_U1A_like cd12246
RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily ...
47-121 2.72e-03

RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily corresponds to the RRM1 of U1A/U2B"/SNF protein family which contains Drosophila sex determination protein SNF and its two mammalian counterparts, U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A) and U2 small nuclear ribonucleoprotein B" (U2 snRNP B" or U2B"), all of which consist of two RNA recognition motifs (RRMs), connected by a variable, flexible linker. SNF is an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila where it is essential in sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). U1A is an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. Moreover, U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins. U2B", initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA, is a unique protein that comprises of the U2 snRNP. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. Moreover, U2B" does not require an auxiliary protein for binding to RNA, and its nuclear transport is independent of U2 snRNA binding.


Pssm-ID: 409692 [Multi-domain]  Cd Length: 78  Bit Score: 34.82  E-value: 2.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665400307  47 VPKINLQANLRTKLQGFGKVqscISVTSEMASKMDLEAFtdvfaVKFERLEVARRAKKMLDAHQFYGGILHISYA 121
Cdd:cd12246   11 IKKDELKRSLYALFSQFGPV---LDIVASKSLKMRGQAF-----VVFKDVESATNALRALQGFPFYGKPMRIQYA 77
 
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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