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Conserved domains on  [gi|197333695|ref|NP_001127949|]
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poly(A)-specific ribonuclease PARN isoform 2 [Homo sapiens]

Protein Classification

R3H_PARN and RRM_PARN domain-containing protein( domain architecture ID 11154053)

R3H_PARN and RRM_PARN domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
 1-329 1.97e-114

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


:

Pssm-ID: 461457  Cd Length: 375  Bit Score: 345.17  E-value: 1.97e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695    1 MDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNrsSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQ 80
Cdd:pfam04857  57 ERFSILQFGLCCFREDEEKSKYTAKPYNFYLFPRTEL--DPDRDFSCQASSLQFLAKHGFDFNKLFYEGIPYLSRAEEEK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695   81 LREQYDEKRSQangagalsyvspNTSKCPVTIPEDqKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKY 160
Cdd:pfam04857 135 LRERLEERQQA------------SPSDIPLLDVED-KEFVERVRSKIKEWLDSGEDKGEKLNIDNPVSRLLLQQLLKHQL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  161 PKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFY 240
Cdd:pfam04857 202 VRVLLVELLSRGKQKVVQVVKKSSEDEELLEKEEKKDEEEERLESAVGFRLVFDALSKSRKPIVGHNGLLDLLFLYQQFY 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  241 CPLPADLSEFKEMTTCVFPRLLDTKLMASTQ-PFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDT----ASEQL 315
Cdd:pfam04857 282 GPLPETLEEFKALIHELFPGIYDTKYLATTDaEFKVRLPSSSLEELFEKLCKENFSSPSVETPPFESDYHDesskYGGKA 361

                         330
                  ....*....|....
gi 197333695  316 HEAGYDAYITGLCF 329
Cdd:pfam04857 362 HEAGYDAYMTGYVF 375
RNA_bind pfam08675
RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ...
 377-451 1.41e-36

RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ribonuclease (PARN).


:

Pssm-ID: 400835  Cd Length: 75  Bit Score: 130.55  E-value: 1.41e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197333695  377 PDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEY 451
Cdd:pfam08675   1 KDPNPSREHVFHVTFPKEWKTSDILQLFSPFGGVYVSWLNDTSAFVSLHRRDQASAVLKTIKYHASYTIQTYAQY 75
 
Name Accession Description Interval E-value
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
 1-329 1.97e-114

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


Pssm-ID: 461457  Cd Length: 375  Bit Score: 345.17  E-value: 1.97e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695    1 MDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNrsSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQ 80
Cdd:pfam04857  57 ERFSILQFGLCCFREDEEKSKYTAKPYNFYLFPRTEL--DPDRDFSCQASSLQFLAKHGFDFNKLFYEGIPYLSRAEEEK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695   81 LREQYDEKRSQangagalsyvspNTSKCPVTIPEDqKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKY 160
Cdd:pfam04857 135 LRERLEERQQA------------SPSDIPLLDVED-KEFVERVRSKIKEWLDSGEDKGEKLNIDNPVSRLLLQQLLKHQL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  161 PKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFY 240
Cdd:pfam04857 202 VRVLLVELLSRGKQKVVQVVKKSSEDEELLEKEEKKDEEEERLESAVGFRLVFDALSKSRKPIVGHNGLLDLLFLYQQFY 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  241 CPLPADLSEFKEMTTCVFPRLLDTKLMASTQ-PFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDT----ASEQL 315
Cdd:pfam04857 282 GPLPETLEEFKALIHELFPGIYDTKYLATTDaEFKVRLPSSSLEELFEKLCKENFSSPSVETPPFESDYHDesskYGGKA 361

                         330
                  ....*....|....
gi 197333695  316 HEAGYDAYITGLCF 329
Cdd:pfam04857 362 HEAGYDAYMTGYVF 375
RNA_bind pfam08675
RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ...
 377-451 1.41e-36

RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ribonuclease (PARN).


Pssm-ID: 400835  Cd Length: 75  Bit Score: 130.55  E-value: 1.41e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197333695  377 PDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEY 451
Cdd:pfam08675   1 KDPNPSREHVFHVTFPKEWKTSDILQLFSPFGGVYVSWLNDTSAFVSLHRRDQASAVLKTIKYHASYTIQTYAQY 75
RRM_PARN cd12428
RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; ...
 383-448 2.08e-35

RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; The subfamily corresponds to the RRM of PARN, also termed deadenylating nuclease, or deadenylation nuclease, or polyadenylate-specific ribonuclease, a processive poly(A)-specific 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. It specifically binds both, the poly(A) tail at the 3' end and the 7-methylguanosine (m7G) cap located at the 5' end of eukaryotic mRNAs, and catalyzes the 3'- to 5'-end deadenylation of single-stranded mRNA with a free 3' hydroxyl group both in the nucleus and in the cytoplasm. PARN belongs to the DEDD superfamily of exonucleases. It contains a nuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an R3H domain. PARN exists as a homodimer. The nuclease domain is involved in the dimerization. RRM and R3H domains are essential for the RNA-binding.


Pssm-ID: 409862 [Multi-domain]  Cd Length: 66  Bit Score: 127.04  E-value: 2.08e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197333695 383 RDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTY 448
Cdd:cd12428    1 RDHVFHLTFPKEWKTSDLYQLFSPFGGIQVSWIDDTSAFVALSDPEQVNIALKTITYHPSYRIRSY 66
R3H_PARN cd02637
R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease ...
 120-185 6.37e-26

R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease from the RNase D family that, in Xenopus, deadenylates a specific class of maternal mRNAs which results in their translational repression. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100066 [Multi-domain]  Cd Length: 65  Bit Score: 100.48  E-value: 6.37e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197333695 120 IDQVVEKIEDLLQSEEnKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDE 185
Cdd:cd02637    1 IDEVIERIEAFLESEE-DDLELEPCNGFQRKLIYQTLEQKYPKGIHVETLETEKKERLIVIEKGDK 65
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
114-183 1.02e-03

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 38.05  E-value: 1.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695   114 EDQKKFIDQVVEKIEDLlQSEENKNLDLEPCTGFQRKLIYQTLSwKYpkGIHVETLETEKKeRYIVISKV 183
Cdd:smart00393  15 PRRREELIELELEIARF-VKSTKESVELPPMNSYERKIVHELAE-KY--GLESESFGEGPK-RRVVISKK 79
 
Name Accession Description Interval E-value
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
 1-329 1.97e-114

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


Pssm-ID: 461457  Cd Length: 375  Bit Score: 345.17  E-value: 1.97e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695    1 MDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNrsSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQ 80
Cdd:pfam04857  57 ERFSILQFGLCCFREDEEKSKYTAKPYNFYLFPRTEL--DPDRDFSCQASSLQFLAKHGFDFNKLFYEGIPYLSRAEEEK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695   81 LREQYDEKRSQangagalsyvspNTSKCPVTIPEDqKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKY 160
Cdd:pfam04857 135 LRERLEERQQA------------SPSDIPLLDVED-KEFVERVRSKIKEWLDSGEDKGEKLNIDNPVSRLLLQQLLKHQL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  161 PKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFY 240
Cdd:pfam04857 202 VRVLLVELLSRGKQKVVQVVKKSSEDEELLEKEEKKDEEEERLESAVGFRLVFDALSKSRKPIVGHNGLLDLLFLYQQFY 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695  241 CPLPADLSEFKEMTTCVFPRLLDTKLMASTQ-PFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDT----ASEQL 315
Cdd:pfam04857 282 GPLPETLEEFKALIHELFPGIYDTKYLATTDaEFKVRLPSSSLEELFEKLCKENFSSPSVETPPFESDYHDesskYGGKA 361

                         330
                  ....*....|....
gi 197333695  316 HEAGYDAYITGLCF 329
Cdd:pfam04857 362 HEAGYDAYMTGYVF 375
RNA_bind pfam08675
RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ...
 377-451 1.41e-36

RNA binding domain; This domain corresponds to the RNA binding domain of Poly(A)-specific ribonuclease (PARN).


Pssm-ID: 400835  Cd Length: 75  Bit Score: 130.55  E-value: 1.41e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197333695  377 PDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEY 451
Cdd:pfam08675   1 KDPNPSREHVFHVTFPKEWKTSDILQLFSPFGGVYVSWLNDTSAFVSLHRRDQASAVLKTIKYHASYTIQTYAQY 75
RRM_PARN cd12428
RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; ...
 383-448 2.08e-35

RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; The subfamily corresponds to the RRM of PARN, also termed deadenylating nuclease, or deadenylation nuclease, or polyadenylate-specific ribonuclease, a processive poly(A)-specific 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. It specifically binds both, the poly(A) tail at the 3' end and the 7-methylguanosine (m7G) cap located at the 5' end of eukaryotic mRNAs, and catalyzes the 3'- to 5'-end deadenylation of single-stranded mRNA with a free 3' hydroxyl group both in the nucleus and in the cytoplasm. PARN belongs to the DEDD superfamily of exonucleases. It contains a nuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an R3H domain. PARN exists as a homodimer. The nuclease domain is involved in the dimerization. RRM and R3H domains are essential for the RNA-binding.


Pssm-ID: 409862 [Multi-domain]  Cd Length: 66  Bit Score: 127.04  E-value: 2.08e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197333695 383 RDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTY 448
Cdd:cd12428    1 RDHVFHLTFPKEWKTSDLYQLFSPFGGIQVSWIDDTSAFVALSDPEQVNIALKTITYHPSYRIRSY 66
R3H_PARN cd02637
R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease ...
 120-185 6.37e-26

R3H domain of Poly(A)-specific ribonuclease (PARN). PARN is a poly(A)-specific 3' exonuclease from the RNase D family that, in Xenopus, deadenylates a specific class of maternal mRNAs which results in their translational repression. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100066 [Multi-domain]  Cd Length: 65  Bit Score: 100.48  E-value: 6.37e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197333695 120 IDQVVEKIEDLLQSEEnKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDE 185
Cdd:cd02637    1 IDEVIERIEAFLESEE-DDLELEPCNGFQRKLIYQTLEQKYPKGIHVETLETEKKERLIVIEKGDK 65
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
 120-182 4.20e-08

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 49.92  E-value: 4.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197333695 120 IDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWkypKGIHVETLETEKKeRYIVISK 182
Cdd:cd02325    1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEY---YGLKSESEGEGPN-RRVVITK 59
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
114-183 1.02e-03

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 38.05  E-value: 1.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695   114 EDQKKFIDQVVEKIEDLlQSEENKNLDLEPCTGFQRKLIYQTLSwKYpkGIHVETLETEKKeRYIVISKV 183
Cdd:smart00393  15 PRRREELIELELEIARF-VKSTKESVELPPMNSYERKIVHELAE-KY--GLESESFGEGPK-RRVVISKK 79
RBD_RRM1_NPL3 cd12340
RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 3 (Npl3p) and similar proteins; ...
 387-433 1.14e-03

RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 3 (Npl3p) and similar proteins; This subfamily corresponds to the RRM1 of Npl3p, also termed mitochondrial targeting suppressor 1 protein, or nuclear polyadenylated RNA-binding protein 1. Npl3p is a major yeast RNA-binding protein that competes with 3'-end processing factors, such as Rna15, for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. It specifically recognizes a class of G/U-rich RNAs. Npl3p is a multi-domain protein containing two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), separated by a short linker and a C-terminal domain rich in glycine, arginine and serine residues.


Pssm-ID: 409777 [Multi-domain]  Cd Length: 69  Bit Score: 37.76  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 197333695 387 LHVT-FPKEWKTSDLYQLFSAFGNIQISWI--DDTSAFVSLSQPEQVKIA 433
Cdd:cd12340    2 LFVRpFPPDTSESAIREIFSPYGPVKEVKMlsDSNFAFVEFEELEDAIRA 51
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 118-182 1.80e-03

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 36.70  E-value: 1.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 197333695  118 KFIDQVVEKIEDLLQSEEnKNLDLEPCTGFQRKLIYQTLSwKYPkgihvetLET----EKKERYIVISK 182
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTG-KSLELPPMSSYERRIIHELAQ-KYG-------LESesegEEPNRRVVVYK 60
RRM3_CELF1-6 cd12362
RNA recognition motif 3 (RRM3) found in CELF/Bruno-like family of RNA binding proteins CELF1, ...
 386-436 6.50e-03

RNA recognition motif 3 (RRM3) found in CELF/Bruno-like family of RNA binding proteins CELF1, CELF2, CELF3, CELF4, CELF5, CELF6 and similar proteins; This subgroup corresponds to the RRM3 of the CUGBP1 and ETR-3-like factors (CELF) or BRUNOL (Bruno-like) proteins, a family of structurally related RNA-binding proteins involved in the regulation of pre-mRNA splicing in the nucleus and in the control of mRNA translation and deadenylation in the cytoplasm. The family contains six members: CELF-1 (also termed BRUNOL-2, or CUG-BP1, or NAPOR, or EDEN-BP), CELF-2 (also termed BRUNOL-3, or ETR-3, or CUG-BP2, or NAPOR-2), CELF-3 (also termed BRUNOL-1, or TNRC4, or ETR-1, or CAGH4, or ER DA4), CELF-4 (also termed BRUNOL-4), CELF-5 (also termed BRUNOL-5), CELF-6 (also termed BRUNOL-6). They all contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The low sequence conservation of the linker region is highly suggestive of a large variety in the co-factors that associate with the various CELF family members. Based on both sequence similarity and function, the CELF family can be divided into two subfamilies, the first containing CELFs 1 and 2, and the second containing CELFs 3, 4, 5, and 6. The different CELF proteins may act through different sites on at least some substrates. Furthermore, CELF proteins may interact with each other in varying combinations to influence alternative splicing in different contexts.


Pssm-ID: 409797 [Multi-domain]  Cd Length: 73  Bit Score: 35.67  E-value: 6.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 197333695 386 VLHVtfPKEWKTSDLYQLFSAFGNIqIS---WIDDTS------AFVSLSQPEQVKIAVNT 436
Cdd:cd12362    3 VYHL--PNEFTDQDLYQLFAPFGNV-VSakvFVDKNTgrskgfGFVSYDNPLSAQAAIKA 59
 
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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