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Conserved domains on  [gi|1775891916|gb|KGN60340|]
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hypothetical protein Csa_000895 [Cucumis sativus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BURP pfam03181
BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. ...
 157-365 9.44e-110

BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus; USPs and USP-like proteins; RD22 from Arabidopsis thaliana; and PG1beta from Lycopersicon esculentum. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid. The function of this domain is unknown.


:

Pssm-ID: 460837  Cd Length: 215  Bit Score: 341.15  E-value: 9.44e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  157 FFLEKDLHPRSKFTLHFPKQ--TTTTTKFLPRRVAKSLPFSSQKLPQILTHFSIPPTSLEAESIRNTIDQCEAPGIVSED 234
Cdd:pfam03181    1 FFLEKDLKPGKKMPLHFPKIdpSAAAASFLPRQVADSIPFSSKKLPEILAMFSIPPGSPMAKAMKDTLRECEAPPIKGET 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  235 KFCATSLESMVDFSTSKMGKK-VTLVSTEVEKDTN-LQAFTVVNLTKKSSVTDSaVACHKLSYPYAVFYCHYAQHTRVYK 312
Cdd:pfam03181   81 KFCATSLESMVDFAVSVLGTRnVRALSTEVPKGSTpLQEYTVAEGVKKIGGDKS-VACHKMPYPYAVFYCHSVPPTRVYM 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  313 VSLLGADGTKADVAAVCHTDTSDWNPKHLAFQVLKVKPGTVPVCHFLPEDHVL 365
Cdd:pfam03181  160 VSLVGEDGTKVEAVAVCHLDTSAWNPDHVAFQVLGVKPGTVPVCHFLPEDHIV 212
BAH super family cl02608
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 387-543 1.47e-52

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


The actual alignment was detected with superfamily member cd04715:

Pssm-ID: 470629  Cd Length: 159  Bit Score: 181.16  E-value: 1.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  387 EFQWGKKKGIGGKKKDVTFYESFTYDGVEYFLYDSVYLYkEGEPEPYIGKLLKIWQNPDKT--KKVKILWFFRSCEILNY 464
Cdd:cd04715      1 EFKWGVKRGEGGKKKDGQFYRSFTYDGVEYRLYDDVYVH-NGDSEPYIGKIIKIYETAIDSgkKKVKVIWFFRPSEIRME 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  465 LGGVDTRE-NELFLASGNGIGLANINSLEVLAGKCNVLCISNDSRNPQPSDEALKKADFVFCRTFDVGKQEVCNEICDKI 543
Cdd:cd04715     80 LKGEPKRHiNEVFLACGRGEGLANINLLESIIGKCNVVCISEDFRNPQPSDGIPTSADFLFPCNFDVGRCVIVDKYDDKI 159
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 814-876 1.48e-03

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: 38.42  E-value: 1.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775891916  814 VLIQNLDPSYTSGEVEDIvwhaFNESCTAKMIQ-KTANSMPHIGQAYVVFKTKEAAEKVVRKLH 876
Cdd:cd00590      1 LFVGNLPPDTTEEDLREL----FSKFGEVVSVRiVRDRDGKSKGFAFVEFESPEDAEKALEALN 60
 
Name Accession Description Interval E-value
BURP pfam03181
BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. ...
 157-365 9.44e-110

BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus; USPs and USP-like proteins; RD22 from Arabidopsis thaliana; and PG1beta from Lycopersicon esculentum. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid. The function of this domain is unknown.


Pssm-ID: 460837  Cd Length: 215  Bit Score: 341.15  E-value: 9.44e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  157 FFLEKDLHPRSKFTLHFPKQ--TTTTTKFLPRRVAKSLPFSSQKLPQILTHFSIPPTSLEAESIRNTIDQCEAPGIVSED 234
Cdd:pfam03181    1 FFLEKDLKPGKKMPLHFPKIdpSAAAASFLPRQVADSIPFSSKKLPEILAMFSIPPGSPMAKAMKDTLRECEAPPIKGET 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  235 KFCATSLESMVDFSTSKMGKK-VTLVSTEVEKDTN-LQAFTVVNLTKKSSVTDSaVACHKLSYPYAVFYCHYAQHTRVYK 312
Cdd:pfam03181   81 KFCATSLESMVDFAVSVLGTRnVRALSTEVPKGSTpLQEYTVAEGVKKIGGDKS-VACHKMPYPYAVFYCHSVPPTRVYM 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  313 VSLLGADGTKADVAAVCHTDTSDWNPKHLAFQVLKVKPGTVPVCHFLPEDHVL 365
Cdd:pfam03181  160 VSLVGEDGTKVEAVAVCHLDTSAWNPDHVAFQVLGVKPGTVPVCHFLPEDHIV 212
BURP smart01045
The BURP domain is found at the C-terminus of several different plant proteins; It was named ...
 156-367 8.02e-70

The BURP domain is found at the C-terminus of several different plant proteins; It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus; USPs and USP-like proteins; RD22 from Arabidopsis thaliana; and PG1beta from Lycopersicon esculentum. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid. The function of this domain is unknown.


Pssm-ID: 214992  Cd Length: 222  Bit Score: 232.88  E-value: 8.02e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   156 LFFLEKDLHPRSKFTLHFPKQTTT-TTKFLPRRVAKSLPFSSQKLPQILTHFSIPPTSLEAESIRNTIDQCEAPGIVSED 234
Cdd:smart01045    2 KFFRENDLKEGTLMLMPFIKDDLMpKRPFLPRQIADLLPFSSSKIDEILRVFSATKNSPMAGIIKETVGECEAPAIEGET 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   235 KFCATSLESMVDFSTSKMGK-KVTLVSTEV---EKDTNLQAFTVVNLTKKSSVTDSAVACHKLSYPYAVFYCHYAQHTRV 310
Cdd:smart01045   82 KRCVTSLESMIDFATSVLGRyVVKVRTTEVvvgSKNKALHNYTVVIAKVKGLNGTKSVSCHQSLYPYAVYYCHSVPGVRV 161

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1775891916   311 YKVSLLGADGTKADV--AAVCHTDTSDWNPKHLAFQVLKVKPGTVPVCHFLPEDHVLQF 367
Cdd:smart01045  162 YEVDLLDPKGMRKINvgPAVCHMDTSAWDANHGAFKVLKSEPGQIPVCHFIPENDMVWV 220
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 387-543 1.47e-52

BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240066  Cd Length: 159  Bit Score: 181.16  E-value: 1.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  387 EFQWGKKKGIGGKKKDVTFYESFTYDGVEYFLYDSVYLYkEGEPEPYIGKLLKIWQNPDKT--KKVKILWFFRSCEILNY 464
Cdd:cd04715      1 EFKWGVKRGEGGKKKDGQFYRSFTYDGVEYRLYDDVYVH-NGDSEPYIGKIIKIYETAIDSgkKKVKVIWFFRPSEIRME 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  465 LGGVDTRE-NELFLASGNGIGLANINSLEVLAGKCNVLCISNDSRNPQPSDEALKKADFVFCRTFDVGKQEVCNEICDKI 543
Cdd:cd04715     80 LKGEPKRHiNEVFLACGRGEGLANINLLESIIGKCNVVCISEDFRNPQPSDGIPTSADFLFPCNFDVGRCVIVDKYDDKI 159
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 420-550 4.39e-08

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 52.69  E-value: 4.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  420 DSVYLYKEGEPEPY-IGKLLKIWQNPD-KTKKVKILWFFRSCEILNYLGGVdTRENELFLAsgngiGLANINSLEVLAGK 497
Cdd:pfam01426    7 DFVLVEPDDADEPYyVARIEELFEDTKnGKKMVRVQWFYRPEETVHRAGKA-FNKDELFLS-----DEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  498 CNVLcisnDSRNPQPSDEALKKADFVFcrtfdvgkqeVCNEICDKIAGVEVKL 550
Cdd:pfam01426   81 CSVL----HKSDLESLDPYKIKEPDDF----------FCELLYDPKTKSFKKL 119
BAH smart00439
Bromo adjacent homology domain;
420-530 3.15e-07

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 50.37  E-value: 3.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   420 DSVYLYKEGEPEPY-IGKLLKIWQNPD--KTKKVKILWFFRSCEI---LNYLggvdTRENELFLASGNgiglaNINSLEV 493
Cdd:smart00439    6 DFVLVEPDDADEPYyIGRIEEIFETKKnsESKMVRVRWFYRPEETvleKAAL----FDKNEVFLSDEY-----DTVPLSD 76

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1775891916   494 LAGKCNVLCISnDSRNPQPSDEALKKADFVFCRTFDV 530
Cdd:smart00439   77 IIGKCNVLYKS-DYPGLRPEGSIGEPDVFFCESAYDP 112
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 814-876 1.48e-03

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: 38.42  E-value: 1.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775891916  814 VLIQNLDPSYTSGEVEDIvwhaFNESCTAKMIQ-KTANSMPHIGQAYVVFKTKEAAEKVVRKLH 876
Cdd:cd00590      1 LFVGNLPPDTTEEDLREL----FSKFGEVVSVRiVRDRDGKSKGFAFVEFESPEDAEKALEALN 60
RRM smart00360
RNA recognition motif;
814-876 3.40e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 37.19  E-value: 3.40e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1775891916   814 VLIQNLDPSYTSGEVEDIvWHAFNESCTAKMIqKTANSMPHIGQAYVVFKTKEAAEKVVRKLH 876
Cdd:smart00360    2 LFVGNLPPDTTEEELREL-FSKFGKVESVRLV-RDKETGKSKGFAFVEFESEEDAEKALEALN 62
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 814-876 9.25e-03

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: 36.06  E-value: 9.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775891916  814 VLIQNLDPSYTSGEVEDIvWHAFNESCTAKMIQK-TANSMphiGQAYVVFKTKEAAEKVVRKLH 876
Cdd:pfam00076    1 LFVGNLPPDTTEEDLKDL-FSKFGPIKSIRLVRDeTGRSK---GFAFVEFEDEEDAEKAIEALN 60
 
Name Accession Description Interval E-value
BURP pfam03181
BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. ...
 157-365 9.44e-110

BURP domain; The BURP domain is found at the C-terminus of several different plant proteins. It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus; USPs and USP-like proteins; RD22 from Arabidopsis thaliana; and PG1beta from Lycopersicon esculentum. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid. The function of this domain is unknown.


Pssm-ID: 460837  Cd Length: 215  Bit Score: 341.15  E-value: 9.44e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  157 FFLEKDLHPRSKFTLHFPKQ--TTTTTKFLPRRVAKSLPFSSQKLPQILTHFSIPPTSLEAESIRNTIDQCEAPGIVSED 234
Cdd:pfam03181    1 FFLEKDLKPGKKMPLHFPKIdpSAAAASFLPRQVADSIPFSSKKLPEILAMFSIPPGSPMAKAMKDTLRECEAPPIKGET 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  235 KFCATSLESMVDFSTSKMGKK-VTLVSTEVEKDTN-LQAFTVVNLTKKSSVTDSaVACHKLSYPYAVFYCHYAQHTRVYK 312
Cdd:pfam03181   81 KFCATSLESMVDFAVSVLGTRnVRALSTEVPKGSTpLQEYTVAEGVKKIGGDKS-VACHKMPYPYAVFYCHSVPPTRVYM 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  313 VSLLGADGTKADVAAVCHTDTSDWNPKHLAFQVLKVKPGTVPVCHFLPEDHVL 365
Cdd:pfam03181  160 VSLVGEDGTKVEAVAVCHLDTSAWNPDHVAFQVLGVKPGTVPVCHFLPEDHIV 212
BURP smart01045
The BURP domain is found at the C-terminus of several different plant proteins; It was named ...
 156-367 8.02e-70

The BURP domain is found at the C-terminus of several different plant proteins; It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus; USPs and USP-like proteins; RD22 from Arabidopsis thaliana; and PG1beta from Lycopersicon esculentum. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid. The function of this domain is unknown.


Pssm-ID: 214992  Cd Length: 222  Bit Score: 232.88  E-value: 8.02e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   156 LFFLEKDLHPRSKFTLHFPKQTTT-TTKFLPRRVAKSLPFSSQKLPQILTHFSIPPTSLEAESIRNTIDQCEAPGIVSED 234
Cdd:smart01045    2 KFFRENDLKEGTLMLMPFIKDDLMpKRPFLPRQIADLLPFSSSKIDEILRVFSATKNSPMAGIIKETVGECEAPAIEGET 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   235 KFCATSLESMVDFSTSKMGK-KVTLVSTEV---EKDTNLQAFTVVNLTKKSSVTDSAVACHKLSYPYAVFYCHYAQHTRV 310
Cdd:smart01045   82 KRCVTSLESMIDFATSVLGRyVVKVRTTEVvvgSKNKALHNYTVVIAKVKGLNGTKSVSCHQSLYPYAVYYCHSVPGVRV 161

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1775891916   311 YKVSLLGADGTKADV--AAVCHTDTSDWNPKHLAFQVLKVKPGTVPVCHFLPEDHVLQF 367
Cdd:smart01045  162 YEVDLLDPKGMRKINvgPAVCHMDTSAWDANHGAFKVLKSEPGQIPVCHFIPENDMVWV 220
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 387-543 1.47e-52

BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240066  Cd Length: 159  Bit Score: 181.16  E-value: 1.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  387 EFQWGKKKGIGGKKKDVTFYESFTYDGVEYFLYDSVYLYkEGEPEPYIGKLLKIWQNPDKT--KKVKILWFFRSCEILNY 464
Cdd:cd04715      1 EFKWGVKRGEGGKKKDGQFYRSFTYDGVEYRLYDDVYVH-NGDSEPYIGKIIKIYETAIDSgkKKVKVIWFFRPSEIRME 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  465 LGGVDTRE-NELFLASGNGIGLANINSLEVLAGKCNVLCISNDSRNPQPSDEALKKADFVFCRTFDVGKQEVCNEICDKI 543
Cdd:cd04715     80 LKGEPKRHiNEVFLACGRGEGLANINLLESIIGKCNVVCISEDFRNPQPSDGIPTSADFLFPCNFDVGRCVIVDKYDDKI 159
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 413-534 2.21e-16

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 76.28  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  413 GVEYFLYDSVYLYKEGEP---EPYIGKLLKIWQNPDKTKKVKILWFFRSCEILNYLGGvDTRENELFLASGNgiglaNIN 489
Cdd:cd04370      1 GITYEVGDSVYVEPDDSIksdPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSP-FALRRELFLSDHL-----DEI 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1775891916  490 SLEVLAGKCNVLCIsNDSRNPQPSDEALKKADFVFCRTFDVGKQE 534
Cdd:cd04370     75 PVESIIGKCKVLFV-SEFEGLKQRPNKIDTDDFFCRLAYDPTTKE 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 420-550 4.39e-08

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 52.69  E-value: 4.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  420 DSVYLYKEGEPEPY-IGKLLKIWQNPD-KTKKVKILWFFRSCEILNYLGGVdTRENELFLAsgngiGLANINSLEVLAGK 497
Cdd:pfam01426    7 DFVLVEPDDADEPYyVARIEELFEDTKnGKKMVRVQWFYRPEETVHRAGKA-FNKDELFLS-----DEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  498 CNVLcisnDSRNPQPSDEALKKADFVFcrtfdvgkqeVCNEICDKIAGVEVKL 550
Cdd:pfam01426   81 CSVL----HKSDLESLDPYKIKEPDDF----------FCELLYDPKTKSFKKL 119
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 420-525 1.78e-07

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 50.86  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  420 DSVYLYKEGEPE-PYIGKLLKIWQNPDKTKKVKILWFFR-----SCEILNYLggvdtrENELFLASGNgiglaNINSLEV 493
Cdd:cd04714      8 DCVLFKSPGRPSlPYVARIESLWEDPEGNMVVRVKWYYRpeetkGGRKPNHG------EKELFASDHQ-----DENSVQT 76

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1775891916  494 LAGKCNVLCISN----DSRNPQPSDealkKADFVFC 525
Cdd:cd04714     77 IEHKCYVLTFAEyerlARVKKKPQD----GVDFYYC 108
BAH smart00439
Bromo adjacent homology domain;
420-530 3.15e-07

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 50.37  E-value: 3.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916   420 DSVYLYKEGEPEPY-IGKLLKIWQNPD--KTKKVKILWFFRSCEI---LNYLggvdTRENELFLASGNgiglaNINSLEV 493
Cdd:smart00439    6 DFVLVEPDDADEPYyIGRIEEIFETKKnsESKMVRVRWFYRPEETvleKAAL----FDKNEVFLSDEY-----DTVPLSD 76

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1775891916   494 LAGKCNVLCISnDSRNPQPSDEALKKADFVFCRTFDV 530
Cdd:smart00439   77 IIGKCNVLYKS-DYPGLRPEGSIGEPDVFFCESAYDP 112
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 406-476 5.23e-06

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240064  Cd Length: 146  Bit Score: 47.46  E-value: 5.23e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1775891916  406 YESFTYDGVEYFLYDSVYLYKEGEPEPYIGKLLKIWQNPDKTKKVKILWFFRSCEI-LNYLGGVDTRE-NELF 476
Cdd:cd04713     11 YTSFEKDGNKYRLEDCVLLVPEDDQKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIeKKKGGNWKAEDpRELF 83
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 409-501 3.66e-05

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240072  Cd Length: 130  Bit Score: 44.36  E-value: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  409 FTYDGVEYFLYDSVYLYKEGEpEPYIGKLLKIWQNPDKTKKVKILWFFRSCEILNYLGGVDTRENELFLASGngiglANI 488
Cdd:cd04721      1 FCRNGVTISVHDFVYVLSEEE-DRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDSVNPREIFLSPN-----LQV 74

                           90
                   ....*....|...
gi 1775891916  489 NSLEVLAGKCNVL 501
Cdd:cd04721     75 ISVECIDGLATVL 87
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 413-524 7.01e-04

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240067  Cd Length: 122  Bit Score: 40.51  E-value: 7.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  413 GVEYFLYDSVYLYKEGEPEPYIGKLLKIWQNPDKTKKVKILWFFRSCE--ILNYLGGVDTRenELFLASgngigLANINS 490
Cdd:cd04716      1 GITYNLGDDAYVQGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDtvIERQATNHDKK--RVFYSE-----IKNDNP 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1775891916  491 LEVLAGKCNVLCISNdSRNPQPSDEALKKADFVF 524
Cdd:cd04716     74 LDCLISKVKILQVPP-NVGTKRKKPNSEKCDYYY 106
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 814-876 1.48e-03

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: 38.42  E-value: 1.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775891916  814 VLIQNLDPSYTSGEVEDIvwhaFNESCTAKMIQ-KTANSMPHIGQAYVVFKTKEAAEKVVRKLH 876
Cdd:cd00590      1 LFVGNLPPDTTEEDLREL----FSKFGEVVSVRiVRDRDGKSKGFAFVEFESPEDAEKALEALN 60
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 413-504 1.74e-03

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 39.49  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  413 GVEYFLYDSVYLYKEGEP-EPYIGKLLKIWQNPDKTKKVKILWFFRSCEILNylggVDTR---ENELFLASgngigLANI 488
Cdd:cd04717      1 GLQYRVGDCVYVANPEDPsKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFH----EPTRkfyKNEVFKSP-----LYET 71

                           90
                   ....*....|....*.
gi 1775891916  489 NSLEVLAGKCNVLCIS 504
Cdd:cd04717     72 VPVEEIVGKCAVMDVK 87
BAH_Orc1p_Yeast cd04720
BAH, or Bromo Adjacent Homology domain, as present in Orc1p, which again is part of the ...
 412-526 2.57e-03

BAH, or Bromo Adjacent Homology domain, as present in Orc1p, which again is part of the Saccharomyces cerevisiae Sir1-origin recognition complex, and as present in Sir3p. The Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240071  Cd Length: 179  Bit Score: 40.09  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775891916  412 DGVEYFLYDSVYLYKEGEPEPYIGKLLKIWQN-PDKTKKVKILWFFRSCEILN--------YLGGVDTRENELFL-ASGN 481
Cdd:cd04720     49 DGLELSVGDTILVKDDVANSPSVYLIHEIRLNtLNNEVELWVMWFLRWFEINParyykqfdPEFRSESNKNELYLtAELS 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1775891916  482 GIGLANINslevlaGKCNVLciSNDSRNPQPSDEALKKADFvFCR 526
Cdd:cd04720    129 EIKLKDII------DKANVL--SESEFNDLSTDDKNGERTF-FCR 164
RRM smart00360
RNA recognition motif;
814-876 3.40e-03

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 37.19  E-value: 3.40e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1775891916   814 VLIQNLDPSYTSGEVEDIvWHAFNESCTAKMIqKTANSMPHIGQAYVVFKTKEAAEKVVRKLH 876
Cdd:smart00360    2 LFVGNLPPDTTEEELREL-FSKFGKVESVRLV-RDKETGKSKGFAFVEFESEEDAEKALEALN 62
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 814-876 9.25e-03

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: 36.06  E-value: 9.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775891916  814 VLIQNLDPSYTSGEVEDIvWHAFNESCTAKMIQK-TANSMphiGQAYVVFKTKEAAEKVVRKLH 876
Cdd:pfam00076    1 LFVGNLPPDTTEEDLKDL-FSKFGPIKSIRLVRDeTGRSK---GFAFVEFEDEEDAEKAIEALN 60
 
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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