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Conserved domains on  [gi|126432546|ref|NP_001075425|]
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A-kinase anchor protein 17B isoform 1 [Mus musculus]

Protein Classification

RRM_AKAP17A domain-containing protein( domain architecture ID 10188106)

RRM_AKAP17A domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 144-262 6.41e-59

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


:

Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 197.11  E-value: 6.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126432546 144 PDSIYFEGLPCKWFAPKGSSgEKPCEEILRVVFESFGKIKNVDIPMLDPYREVMTGGSFGGLNFG-LQTFEAFIQYQEST 222
Cdd:cd12264    4 PDTIHLEGLPCKWFAVPRSS-DKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGgHLHFEAYVQYEEYD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 126432546 223 DFIKAMESLRGMKLMLKGDDGKALACNIKVMFDTTKHFSE 262
Cdd:cd12264   83 GFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
 
Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 144-262 6.41e-59

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 197.11  E-value: 6.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126432546 144 PDSIYFEGLPCKWFAPKGSSgEKPCEEILRVVFESFGKIKNVDIPMLDPYREVMTGGSFGGLNFG-LQTFEAFIQYQEST 222
Cdd:cd12264    4 PDTIHLEGLPCKWFAVPRSS-DKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGgHLHFEAYVQYEEYD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 126432546 223 DFIKAMESLRGMKLMLKGDDGKALACNIKVMFDTTKHFSE 262
Cdd:cd12264   83 GFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
RRM smart00360
RNA recognition motif;
169-239 1.29e-05

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.12  E-value: 1.29e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126432546   169 EEILRVVFESFGKIKNVDIPmldpyREVMTGGSFGglnfglqtfEAFIQYQESTDFIKAMESLRGMKLMLK 239
Cdd:smart00360  13 EEELRELFSKFGKVESVRLV-----RDKETGKSKG---------FAFVEFESEEDAEKALEALNGKELDGR 69
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 169-239 1.85e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 40.68  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126432546  169 EEILRVVFESFGKIKNVDIPMLDpyrevmTGGSFGglnfglqtfEAFIQYQESTDFIKAMESLRGMKLMLK 239
Cdd:pfam00076  12 EEDLKDLFSKFGPIKSIRLVRDE------TGRSKG---------FAFVEFEDEEDAEKAIEALNGKELGGR 67
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 169-236 2.99e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.44  E-value: 2.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126432546  169 EEILRVVFESFGKIKNVDIPMlDPYrevmTGGSFGglnFGlqtfeaFIQYQESTDFIKAMESLRGMKL 236
Cdd:TIGR01622 228 EQDLRQIFEPFGEIEFVQLQK-DPE----TGRSKG---YG------FIQFRDAEQAKEALEKMNGFEL 281
 
Name Accession Description Interval E-value
RRM_AKAP17A cd12264
RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar ...
 144-262 6.41e-59

RNA recognition motif (RRM) found in A-kinase anchor protein 17A (AKAP-17A) and similar proteins; This subfamily corresponds to the RRM domain of AKAP-17A, also termed 721P, or splicing factor, arginine/serine-rich 17A (SFRS17A). It was originally reported as the pseudoautosomal or X inactivation escape gene 7 (XE7) and as B-lymphocyte antigen precursor. It has been suggested that AKAP-17A is an alternative splicing factor and an SR-related splicing protein that interacts with the classical SR protein ASF/SF2 and the SR-related factor ZNF265. Additional studies have indicated that AKAP-17A is a dual-specific protein kinase A anchoring protein (AKAP) that can bind both type I and type II protein kinase A (PKA) with high affinity and co-localizes with the catalytic subunit of PKA in nuclear speckles as well as the splicing factor SC35 in splicing factor compartments. It is involved in regulation of pre-mRNA splicing possibly by docking a pool of PKA in splicing factor compartments. AKAP-17A contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409708 [Multi-domain]  Cd Length: 122  Bit Score: 197.11  E-value: 6.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126432546 144 PDSIYFEGLPCKWFAPKGSSgEKPCEEILRVVFESFGKIKNVDIPMLDPYREVMTGGSFGGLNFG-LQTFEAFIQYQEST 222
Cdd:cd12264    4 PDTIHLEGLPCKWFAVPRSS-DKPSENVLRKVFEKFGKIRNVDIPMLDPYRKEMDGNGFDTFSFGgHLHFEAYVQYEEYD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 126432546 223 DFIKAMESLRGMKLMLKGDDGKALACNIKVMFDTTKHFSE 262
Cdd:cd12264   83 GFVKAMDALRGMKLMYKGEDGKALAANIKVDFDKTKHLSE 122
RRM2_RBM23_RBM39 cd12284
RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein RBM23, RBM39 and ...
 169-236 1.57e-07

RNA recognition motif 2 (RRM2) found in vertebrate RNA-binding protein RBM23, RBM39 and similar proteins; This subfamily corresponds to the RRM2 of RBM39 (also termed HCC1), a nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Although the cellular function of RBM23 remains unclear, it shows high sequence homology to RBM39 and contains two RRMs. It may possibly function as a pre-mRNA splicing factor.


Pssm-ID: 409726 [Multi-domain]  Cd Length: 78  Bit Score: 49.55  E-value: 1.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126432546 169 EEILRVVFESFGKIKNVDIPmldpyREVMTGGSFGglnFGlqtfeaFIQYQESTDFIKAMESLRGMKL 236
Cdd:cd12284   12 EDMLRGIFEPFGKIEFVQLQ-----KDPETGRSKG---YG------FIQFRDAEDAKKALEQLNGFEL 65
RRM smart00360
RNA recognition motif;
169-239 1.29e-05

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.12  E-value: 1.29e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126432546   169 EEILRVVFESFGKIKNVDIPmldpyREVMTGGSFGglnfglqtfEAFIQYQESTDFIKAMESLRGMKLMLK 239
Cdd:smart00360  13 EEELRELFSKFGKVESVRLV-----RDKETGKSKG---------FAFVEFESEEDAEKALEALNGKELDGR 69
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 169-239 1.85e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 40.68  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126432546  169 EEILRVVFESFGKIKNVDIPMLDpyrevmTGGSFGglnfglqtfEAFIQYQESTDFIKAMESLRGMKLMLK 239
Cdd:pfam00076  12 EEDLKDLFSKFGPIKSIRLVRDE------TGRSKG---------FAFVEFEDEEDAEKAIEALNGKELGGR 67
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 169-237 4.00e-04

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).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 39.57  E-value: 4.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126432546 169 EEILRVVFESFGKIKNVDIPMlDPyrevmTGGSFGglnfglqtfEAFIQYQESTDFIKAMESLRGMKLM 237
Cdd:cd00590   12 EEDLRELFSKFGEVVSVRIVR-DR-----DGKSKG---------FAFVEFESPEDAEKALEALNGTELG 65
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 169-236 2.99e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.44  E-value: 2.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126432546  169 EEILRVVFESFGKIKNVDIPMlDPYrevmTGGSFGglnFGlqtfeaFIQYQESTDFIKAMESLRGMKL 236
Cdd:TIGR01622 228 EQDLRQIFEPFGEIEFVQLQK-DPE----TGRSKG---YG------FIQFRDAEQAKEALEKMNGFEL 281
 
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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