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Conserved domains on  [gi|41054625|ref|NP_955870|]
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serine/arginine-rich splicing factor 11 [Danio rerio]

Protein Classification

serine/arginine-rich splicing factor 11( domain architecture ID 10189854)

serine/arginine-rich splicing factor 11 (SRSF11) may function in pre-mRNA splicing

CATH:  3.30.70.330
Gene Symbol:  SRSF11
Gene Ontology:  GO:0003723|GO:0008380|GO:0006397
PubMed:  15853797|18515081|22278943
SCOP:  3000110

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_SRSF11 cd12518
RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and ...
 8-87 3.41e-53

RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and similar proteins; This subgroup corresponds to the RRM of SRSF11, also termed arginine-rich 54 kDa nuclear protein (SRp54 or p54), which belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family). It is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SRSF11 has been identified as a tau exon 10 splicing repressor. It interacts with a purine-rich element in exon 10, and suppresses exon 10 inclusion by antagonizing Tra2beta, an SR-domain-containing protein that enhances exon 10 inclusion. SRSF11 is a unique SR family member and may regulate the alternative splicing in a tissue- and substrate-dependent manner. It can directly interact with the U2 auxiliary factor 65-kDa subunit (U2AF65), a protein associated with the 3' splice site. In addition, unlike the typical SR proteins, SRSF11 associates with other SR proteins but not with the U1 small nuclear ribonucleoprotein U1-70K or the U2 auxiliary factor 35-kDa subunit (U2AF35). SREK1 has unique properties in regulating alternative splicing of different pre-mRNAs; it promotes the use of the distal 5' splice site in E1A pre-mRNA alternative splicing. It also inhibits cryptic splice site selection on the beta-globin pre-mRNA containing competing 5' splice sites. SREK1 contains an RNA recognition motif (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and one serine-arginine (SR)-rich domains (SR domains).


:

Pssm-ID: 409940 [Multi-domain]  Cd Length: 80  Bit Score: 172.92  E-value: 3.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625   8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPVTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVPFAEG 87
Cdd:cd12518   1 VIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVTSRVCFVKFHEPDSAVVAQHLTNTVFVDRALIVVPYAEG 80
 
Name Accession Description Interval E-value
RRM_SRSF11 cd12518
RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and ...
 8-87 3.41e-53

RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and similar proteins; This subgroup corresponds to the RRM of SRSF11, also termed arginine-rich 54 kDa nuclear protein (SRp54 or p54), which belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family). It is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SRSF11 has been identified as a tau exon 10 splicing repressor. It interacts with a purine-rich element in exon 10, and suppresses exon 10 inclusion by antagonizing Tra2beta, an SR-domain-containing protein that enhances exon 10 inclusion. SRSF11 is a unique SR family member and may regulate the alternative splicing in a tissue- and substrate-dependent manner. It can directly interact with the U2 auxiliary factor 65-kDa subunit (U2AF65), a protein associated with the 3' splice site. In addition, unlike the typical SR proteins, SRSF11 associates with other SR proteins but not with the U1 small nuclear ribonucleoprotein U1-70K or the U2 auxiliary factor 35-kDa subunit (U2AF35). SREK1 has unique properties in regulating alternative splicing of different pre-mRNAs; it promotes the use of the distal 5' splice site in E1A pre-mRNA alternative splicing. It also inhibits cryptic splice site selection on the beta-globin pre-mRNA containing competing 5' splice sites. SREK1 contains an RNA recognition motif (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and one serine-arginine (SR)-rich domains (SR domains).


Pssm-ID: 409940 [Multi-domain]  Cd Length: 80  Bit Score: 172.92  E-value: 3.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625   8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPVTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVPFAEG 87
Cdd:cd12518   1 VIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVTSRVCFVKFHEPDSAVVAQHLTNTVFVDRALIVVPYAEG 80
RRM smart00360
RNA recognition motif;
8-81 1.36e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 40.27  E-value: 1.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054625      8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPvtSRVCFVKFHEPESVG-VSQHLTNTVFVDRALIV 81
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVESVRLVRDKETGKS--KGFAFVEFESEEDAEkALEALNGKELDGRPLKV 73
PLN03120 PLN03120
nucleic acid binding protein; Provisional
 4-95 3.55e-04

nucleic acid binding protein; Provisional


Pssm-ID: 215588  Cd Length: 260  Bit Score: 42.34  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625    4 SSTSVIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDsplpvTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVP 83
Cdd:PLN03120   2 MQVRTVKVSNVSLKATERDIKEFFSFSGDIEYVEMQSENE-----RSQIAYVTFKDPQGAETALLLSGATIVDQSVTITP 76

                         90
                 ....*....|..
gi 41054625   84 FAEGVIPDESKA 95
Cdd:PLN03120  77 AEDYQLPPEALA 88
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 11-62 6.80e-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: 37.98  E-value: 6.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41054625    11 VTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPlpvTSRVCFVKFHEPES 62
Cdd:pfam00076   3 VGNLPPDTTEEDLKDLFSKFGPIKSIRLVRDETGR---SKGFAFVEFEDEED 51
 
Name Accession Description Interval E-value
RRM_SRSF11 cd12518
RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and ...
 8-87 3.41e-53

RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11) and similar proteins; This subgroup corresponds to the RRM of SRSF11, also termed arginine-rich 54 kDa nuclear protein (SRp54 or p54), which belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family). It is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SRSF11 has been identified as a tau exon 10 splicing repressor. It interacts with a purine-rich element in exon 10, and suppresses exon 10 inclusion by antagonizing Tra2beta, an SR-domain-containing protein that enhances exon 10 inclusion. SRSF11 is a unique SR family member and may regulate the alternative splicing in a tissue- and substrate-dependent manner. It can directly interact with the U2 auxiliary factor 65-kDa subunit (U2AF65), a protein associated with the 3' splice site. In addition, unlike the typical SR proteins, SRSF11 associates with other SR proteins but not with the U1 small nuclear ribonucleoprotein U1-70K or the U2 auxiliary factor 35-kDa subunit (U2AF35). SREK1 has unique properties in regulating alternative splicing of different pre-mRNAs; it promotes the use of the distal 5' splice site in E1A pre-mRNA alternative splicing. It also inhibits cryptic splice site selection on the beta-globin pre-mRNA containing competing 5' splice sites. SREK1 contains an RNA recognition motif (RRM), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and one serine-arginine (SR)-rich domains (SR domains).


Pssm-ID: 409940 [Multi-domain]  Cd Length: 80  Bit Score: 172.92  E-value: 3.41e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625   8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPVTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVPFAEG 87
Cdd:cd12518   1 VIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVTSRVCFVKFHEPDSAVVAQHLTNTVFVDRALIVVPYAEG 80
RRM_SRSF11_SREK1 cd12259
RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11), ...
 8-83 1.10e-41

RNA recognition motif (RRM) found in serine/arginine-rich splicing factor 11 (SRSF11), splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins; This subfamily corresponds to the RRM domain of SRSF11 (SRp54 or p54), SREK1 ( SFRS12 or SRrp86) and similar proteins, a group of proteins containing regions rich in serine-arginine dipeptides (SR protein family). These are involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. SR proteins have been identified as crucial regulators of alternative splicing. Different SR proteins display different substrate specificity, have distinct functions in alternative splicing of different pre-mRNAs, and can even negatively regulate splicing. All SR family members are characterized by the presence of one or two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and the C-terminal regions rich in serine and arginine dipeptides (SR domains). The RRM domain is responsible for RNA binding and specificity in both alternative and constitutive splicing. In contrast, SR domains are thought to be protein-protein interaction domains that are often interchangeable.


Pssm-ID: 409704 [Multi-domain]  Cd Length: 76  Bit Score: 142.46  E-value: 1.10e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054625   8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPVTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVP 83
Cdd:cd12259   1 VVQVTNVSPQATEEQMRTLFGFIGKIEELRLYPSEDDLAPVLSKVCFVKYEDPEDVAVALHLTNTVFIDRALIVIP 76
RRM1_SREK1 cd12519
RNA recognition motif 1 (RRM1) found in splicing regulatory glutamine/lysine-rich protein 1 ...
 8-87 2.58e-38

RNA recognition motif 1 (RRM1) found in splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins; This subgroup corresponds to the RRM1 of SREK1, also termed serine/arginine-rich-splicing regulatory protein 86-kDa (SRrp86), or splicing factor arginine/serine-rich 12 (SFRS12), or splicing regulatory protein 508 amino acid (SRrp508). SREK1 belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family), and is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. It is a unique SR family member and may play a crucial role in determining tissue specific patterns of alternative splicing. SREK1 can alter splice site selection by both positively and negatively modulating the activity of other SR proteins. For instance, SREK1 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. In addition, SREK1 generally contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and two serine-arginine (SR)-rich domains (SR domains) separated by an unusual glutamic acid-lysine (EK) rich region. The RRM and SR domains are highly conserved among other members of the SR superfamily. However, the EK domain is unique to SREK1; plays a modulatory role controlling SR domain function by involvement in the inhibition of both constitutive and alternative splicing and in the selection of splice-site.


Pssm-ID: 409941 [Multi-domain]  Cd Length: 80  Bit Score: 133.99  E-value: 2.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625   8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPVTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVPFAEG 87
Cdd:cd12519   1 VIQVTNLSAAVTSDQMRTLFSFLGDIEELRLYPPDNAPLAFSSKVCYVKYREPSSVGVAQHLTNTVFIDRALIVVPCAEG 80
RRM_Vip1_like cd12269
RNA recognition motif (RRM) found in a group of uncharacterized plant proteins similar to ...
 9-82 9.97e-07

RNA recognition motif (RRM) found in a group of uncharacterized plant proteins similar to fission yeast Vip1; This subfamily corresponds to the Vip1-like, uncharacterized proteins found in plants. Although their biological roles remain unclear, these proteins show high sequence similarity to the fission yeast Vip1. Like Vip1 protein, members in this family contain an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409712 [Multi-domain]  Cd Length: 69  Bit Score: 45.99  E-value: 9.97e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054625   9 IQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSplpvtSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVV 82
Cdd:cd12269   1 VEVTNVSPLATERDLHEFFSFSGDIEHIEIQREGEQ-----SRIAFVTFKDPYALETAVLLSGATIVDQRVTIT 69
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 9-81 4.20e-05

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: 41.50  E-value: 4.20e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054625   9 IQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDsplPVTSRVCFVKFHEPESVG--VsQHLTNTVFVDRALIV 81
Cdd:cd00590   1 LFVGNLPPDTTEEDLRELFSKFGEVVSVRIVRDRD---GKSKGFAFVEFESPEDAEkaL-EALNGTELGGRPLKV 71
RRM smart00360
RNA recognition motif;
8-81 1.36e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 40.27  E-value: 1.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054625      8 VIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPLPvtSRVCFVKFHEPESVG-VSQHLTNTVFVDRALIV 81
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVESVRLVRDKETGKS--KGFAFVEFESEEDAEkALEALNGKELDGRPLKV 73
RRM_eIF3G_like cd12408
RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 subunit G ...
 9-62 2.61e-04

RNA recognition motif (RRM) found in eukaryotic translation initiation factor 3 subunit G (eIF-3G) and similar proteins; This subfamily corresponds to the RRM of eIF-3G and similar proteins. eIF-3G, also termed eIF-3 subunit 4, or eIF-3-delta, or eIF3-p42, or eIF3-p44, is the RNA-binding subunit of eIF3, a large multisubunit complex that plays a central role in the initiation of translation by binding to the 40 S ribosomal subunit and promoting the binding of methionyl-tRNAi and mRNA. eIF-3G binds 18 S rRNA and beta-globin mRNA, and therefore appears to be a nonspecific RNA-binding protein. eIF-3G is one of the cytosolic targets and interacts with mature apoptosis-inducing factor (AIF). eIF-3G contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). This family also includes yeast eIF3-p33, a homolog of vertebrate eIF-3G, plays an important role in the initiation phase of protein synthesis in yeast. It binds both, mRNA and rRNA, fragments due to an RRM near its C-terminus.


Pssm-ID: 409842 [Multi-domain]  Cd Length: 76  Bit Score: 39.41  E-value: 2.61e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054625   9 IQVTNVSPSSTAEQMRTLFGFIGSIDelRLFPPDDsplPVTSR---VCFVKFHEPES 62
Cdd:cd12408   2 IRVTNLSEDATEEDLRELFRPFGPIS--RVYLAKD---KETGQskgFAFVTFETRED 53
RRM2_SREK1 cd12260
RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 ...
 9-81 3.14e-04

RNA recognition motif 2 (RRM2) found in splicing regulatory glutamine/lysine-rich protein 1 (SREK1) and similar proteins; This subfamily corresponds to the RRM2 of SREK1, also termed serine/arginine-rich-splicing regulatory protein 86-kDa (SRrp86), or splicing factor arginine/serine-rich 12 (SFRS12), or splicing regulatory protein 508 amino acid (SRrp508). SREK1 belongs to a family of proteins containing regions rich in serine-arginine dipeptides (SR proteins family), which is involved in bridge-complex formation and splicing by mediating protein-protein interactions across either introns or exons. It is a unique SR family member and it may play a crucial role in determining tissue specific patterns of alternative splicing. SREK1 can alter splice site selection by both positively and negatively modulating the activity of other SR proteins. For instance, SREK1 can activate SRp20 and repress SC35 in a dose-dependent manner both in vitro and in vivo. In addition, SREK1 contains two (some contain only one) RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and two serine-arginine (SR)-rich domains (SR domains) separated by an unusual glutamic acid-lysine (EK) rich region. The RRM and SR domains are highly conserved among other members of the SR superfamily. However, the EK domain is unique to SREK1. It plays a modulatory role controlling SR domain function by involvement in the inhibition of both constitutive and alternative splicing and in the selection of splice-site.


Pssm-ID: 409705 [Multi-domain]  Cd Length: 85  Bit Score: 39.60  E-value: 3.14e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054625   9 IQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPlpvtSRVCFVKFHEPESVGVSQHLTNTVFVDRALIV 81
Cdd:cd12260   7 VYVGNLDPSTTADQLLEFFSQAGEVKYVRMAGDETQP----TRYAFVEFAEQTSVINALKLNGKMFGGRPLKV 75
PLN03120 PLN03120
nucleic acid binding protein; Provisional
 4-95 3.55e-04

nucleic acid binding protein; Provisional


Pssm-ID: 215588  Cd Length: 260  Bit Score: 42.34  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054625    4 SSTSVIQVTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDsplpvTSRVCFVKFHEPESVGVSQHLTNTVFVDRALIVVP 83
Cdd:PLN03120   2 MQVRTVKVSNVSLKATERDIKEFFSFSGDIEYVEMQSENE-----RSQIAYVTFKDPQGAETALLLSGATIVDQSVTITP 76

                         90
                 ....*....|..
gi 41054625   84 FAEGVIPDESKA 95
Cdd:PLN03120  77 AEDYQLPPEALA 88
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 11-62 6.80e-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: 37.98  E-value: 6.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41054625    11 VTNVSPSSTAEQMRTLFGFIGSIDELRLFPPDDSPlpvTSRVCFVKFHEPES 62
Cdd:pfam00076   3 VGNLPPDTTEEDLKDLFSKFGPIKSIRLVRDETGR---SKGFAFVEFEDEED 51
 
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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