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Conserved domains on  [gi|25151685|ref|NP_498223|]
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Calcipressin-like protein [Caenorhabditis elegans]

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 ...
 41-201 1.82e-37

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 pfam04847:

Pssm-ID: 473069  Cd Length: 183  Bit Score: 128.46  E-value: 1.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685    41 VFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAK--LIVQGFSFKGHELKAFFAQ--RIYMSANSQM 116
Cdd:pfam04847   1 DFVDQDNKEKLRALFRTYDDIVTWQPLKSFRRIIVNFSSEEAAARARiqLHWEKTEFLGKKLRLYFAQpqTIQRDLAKSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685   117 LSPPPLEKQFLISPPCSPPVGWEQTKDMPP--VVCNFDLMARLASFAIDEKYEVHNGDELTPAIIV-----HPCETPIDV 189
Cdd:pfam04847  81 LAPPQPEKQFLISPPASPPVGWEQKEEDAPnrHVLNEDLQYALAKLGPGEKYQLHAGTDTTPSVVVtllksHVGESEIDE 160

                         170
                  ....*....|..
gi 25151685   190 PSAIEMPRTPRP 201
Cdd:pfam04847 161 EETNGDGDTPRP 172
 
Name Accession Description Interval E-value
Calcipressin pfam04847
Calcipressin; Calcipressin is also known as calcineurin-binding protein, since it inhibits ...
 41-201 1.82e-37

Calcipressin; Calcipressin is also known as calcineurin-binding protein, since it inhibits calcineurin-mediated transcriptional modulation by binding to calcineurin's catalytic domain.


Pssm-ID: 282674  Cd Length: 183  Bit Score: 128.46  E-value: 1.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685    41 VFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAK--LIVQGFSFKGHELKAFFAQ--RIYMSANSQM 116
Cdd:pfam04847   1 DFVDQDNKEKLRALFRTYDDIVTWQPLKSFRRIIVNFSSEEAAARARiqLHWEKTEFLGKKLRLYFAQpqTIQRDLAKSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685   117 LSPPPLEKQFLISPPCSPPVGWEQTKDMPP--VVCNFDLMARLASFAIDEKYEVHNGDELTPAIIV-----HPCETPIDV 189
Cdd:pfam04847  81 LAPPQPEKQFLISPPASPPVGWEQKEEDAPnrHVLNEDLQYALAKLGPGEKYQLHAGTDTTPSVVVtllksHVGESEIDE 160

                         170
                  ....*....|..
gi 25151685   190 PSAIEMPRTPRP 201
Cdd:pfam04847 161 EETNGDGDTPRP 172
RRM_RCAN_like cd12434
RNA recognition motif (RRM) found in regulators of calcineurin (RCANs) and similar proteins; ...
 32-106 1.29e-30

RNA recognition motif (RRM) found in regulators of calcineurin (RCANs) and similar proteins; This subfamily corresponds to the RRM of RCANs, a novel family of calcineurin regulators that are key factors contributing to Down syndrome in humans. They can stimulate and inhibit the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C) signaling in vivo through direct interactions with its catalytic subunit. Overexpressed RCANs may bind and inhibit calcineurin. In contrast, low levels of phosphorylated RCANs may stimulate the calcineurin signaling. RCANs are characterized by harboring a central short, unique serine-proline motif containing FLIISPPxSPP box, which is strongly conserved from yeast to human but is absent in bacteria. They consist of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function.


Pssm-ID: 409868 [Multi-domain]  Cd Length: 75  Bit Score: 107.32  E-value: 1.29e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151685  32 IIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQ 106
Cdd:cd12434   1 LIVTNVPSEVFDNAELKEAFESLFRTYGEIATFVYLKSFRRARVIFSSPEEAALARIELHGTVFLGSELRVYFGQ 75
 
Name Accession Description Interval E-value
Calcipressin pfam04847
Calcipressin; Calcipressin is also known as calcineurin-binding protein, since it inhibits ...
 41-201 1.82e-37

Calcipressin; Calcipressin is also known as calcineurin-binding protein, since it inhibits calcineurin-mediated transcriptional modulation by binding to calcineurin's catalytic domain.


Pssm-ID: 282674  Cd Length: 183  Bit Score: 128.46  E-value: 1.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685    41 VFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAK--LIVQGFSFKGHELKAFFAQ--RIYMSANSQM 116
Cdd:pfam04847   1 DFVDQDNKEKLRALFRTYDDIVTWQPLKSFRRIIVNFSSEEAAARARiqLHWEKTEFLGKKLRLYFAQpqTIQRDLAKSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685   117 LSPPPLEKQFLISPPCSPPVGWEQTKDMPP--VVCNFDLMARLASFAIDEKYEVHNGDELTPAIIV-----HPCETPIDV 189
Cdd:pfam04847  81 LAPPQPEKQFLISPPASPPVGWEQKEEDAPnrHVLNEDLQYALAKLGPGEKYQLHAGTDTTPSVVVtllksHVGESEIDE 160

                         170
                  ....*....|..
gi 25151685   190 PSAIEMPRTPRP 201
Cdd:pfam04847 161 EETNGDGDTPRP 172
RRM_RCAN_like cd12434
RNA recognition motif (RRM) found in regulators of calcineurin (RCANs) and similar proteins; ...
 32-106 1.29e-30

RNA recognition motif (RRM) found in regulators of calcineurin (RCANs) and similar proteins; This subfamily corresponds to the RRM of RCANs, a novel family of calcineurin regulators that are key factors contributing to Down syndrome in humans. They can stimulate and inhibit the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C) signaling in vivo through direct interactions with its catalytic subunit. Overexpressed RCANs may bind and inhibit calcineurin. In contrast, low levels of phosphorylated RCANs may stimulate the calcineurin signaling. RCANs are characterized by harboring a central short, unique serine-proline motif containing FLIISPPxSPP box, which is strongly conserved from yeast to human but is absent in bacteria. They consist of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function.


Pssm-ID: 409868 [Multi-domain]  Cd Length: 75  Bit Score: 107.32  E-value: 1.29e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25151685  32 IIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQ 106
Cdd:cd12434   1 LIVTNVPSEVFDNAELKEAFESLFRTYGEIATFVYLKSFRRARVIFSSPEEAALARIELHGTVFLGSELRVYFGQ 75
RRM_RCAN1 cd12708
RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 1 (RCAN1); This ...
 31-124 5.06e-18

RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 1 (RCAN1); This subgroup corresponds to the RRM of RCAN1, also termed calcipressin-1, or Adapt78, or Down syndrome critical region protein 1, or myocyte-enriched calcineurin-interacting protein 1 (MCIP1), encoded by the Down syndrome critical region 1 (DSCR1) gene that is abundantly expressed in human brain, heart and muscles. Overexpressed RCAN1 functions as an inhibitor of the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), and is associated with Alzheimer's disease (AD) and Down syndrome (DS). RCAN1 can be phosphorylated by several kinases such as big MAP kinase 1 (BMK1), glycogen synthase kinase-3 (GSK-3), NF-kappaB inducing kinase (NIK), and protein kinase A (PKA). The phosphorylation of RCAN1 can positively or negatively regulate calcineurin-mediated gene transcription, and also affect its protein stability in the ubiquitin-proteasome pathway. RCAN1 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function.


Pssm-ID: 410107  Cd Length: 93  Bit Score: 75.27  E-value: 5.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151685  31 AIIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQRIYM 110
Cdd:cd12708   2 SLVACVADTDVFTDSETRAKFESLFRAYDKDATFQFFKSFKRVRINFSNPISAAEARIRLHKTEFNGKEIKLYFAQTLHI 81

                        90
                ....*....|....
gi 25151685 111 SanSQMLSPPPLEK 124
Cdd:cd12708  82 G--SPHLAPPNPDK 93
RRM_RCAN3 cd12710
RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 3 (RCAN3); This ...
 31-106 5.43e-14

RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 3 (RCAN3); This subgroup corresponds to the RRM of RCAN3, also termed calcipressin-3, or Down syndrome candidate region 1-like protein 2 (DSCR1L2), or myocyte-enriched calcineurin-interacting protein 3 (MCIP3), encoded by a ubiquitously expressed DSCR1L2 gene. Overexpressed RCAN3 binds and inhibits the Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), and further down-regulates nuclear factor of activated T cells (NFAT)-dependent cytokine gene expression in activated human Jurkat T cells. Moreover, RCAN3 interacts with cardiac troponin I (TNNI3), a heart-specific inhibitory subunit of the troponin complex, and may play a role in cardiac contraction. RCAN3 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function.


Pssm-ID: 410109  Cd Length: 77  Bit Score: 64.57  E-value: 5.43e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25151685  31 AIIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQ 106
Cdd:cd12710   2 ALFACSVHEAVFEDQEQRERFEALFRIYDNQVTFQLFKSFRRVRINFSNPEAAARARIELHESDFNGKKLKLYFAQ 77
RRM_RCAN2 cd12709
RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 2 (RCAN2); This ...
 30-106 7.50e-13

RNA recognition motif (RRM) found in vertebrate regulator of calcineurin 2 (RCAN2); This subgroup corresponds to the RRM of RCAN2, also termed calcipressin-2, or Down syndrome candidate region 1-like 1 (DSCR1L1), or myocyte-enriched calcineurin-interacting protein 2 (MCIP2), or thyroid hormone-responsive protein ZAKI-4, encoded by a novel thyroid hormone-responsive gene ZAKI-4 that is abundantly expressed in human brain, heart and muscles. RCAN2 binds to the catalytic subunit of Ca2+/calmodulin-dependent phosphatase calcineurin (also termed PP2B or PP3C), calcineurin A, and inhibits its phosphatase activity through its C-terminal region. RCAN2 consists of an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a highly conserved SP repeat domain containing the phosphorylation site by GSK-3, a well-known PxIxIT motif responsible for docking many substrates to calcineurin, and an unrecognized C-terminal TxxP motif of unknown function.


Pssm-ID: 410108  Cd Length: 77  Bit Score: 61.50  E-value: 7.50e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151685  30 NAIIVTQVPEDVFDNKQDKANFSSLFTQIEKDIHFDFLRSFRRVRVIFSSPENATAAKLIVQGFSFKGHELKAFFAQ 106
Cdd:cd12709   1 STLFACNVDQEVFTSQESKEKFEALFLAYDDCVTFQLFKSFRRVRINFSNPKAAARARIELHETQFRGKKLKLYFAQ 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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