Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Binds DNA specifically (PMID: 10066757)
Previous Annotations
Source
Annotation
TF-CAT classification
No PMIDS:
Vaquerizas 2009 TF classification
"a " Has direct evidence of TF function;
"b " Has evidence for an orthologous TF;
"c " contains likely DBDs, but has no functional evidence;
"x " is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription;
"other " category contains proteins without clear DBDs they curated from external sources.
x
CisBP considers it as a TF?
No
TFclass considers it as a TF?
No
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
No
GO-Info
Initial Assessment
1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding;
1a2 There is high confidence data for a close ortholog (as defined in CisBP);
2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model;
2a2 There is lower confidence evidence for an close ortholog;
3a There is decent circumstantial evidence for its role as a TF or not;
4a Two or more datasets predict it as a TF;
5a One of the source datasets predicts is as a TF
1a1, Direct HQ evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
{"regions": [{"startStyle": "straight", "end": 1028, "endStyle": "straight", "aliStart": 386, "text": "RAG1", "colour": "#9999ff", "aliEnd": 1021, "start": 384, "href": "http://pfam.xfam.org/family/PF12940.5", "type": "pfama", "display": "true", "metadata": {"end": 1028, "description": "This family is one of the two different components of the RAG1-RAG2 V(D)J recombinase complex. The RAG complex, consisting of two RAG1 and two RAG2 proteins is a multi-protein complex that mediates DNA cleavage during V(D)J (variable-diversity-joining) recombination [2]. RAG1 mediates DNA-binding to the conserved recombination signal sequences (RSS) [3]. Many of the proteins in this family are fragments. Solution of the structure of the complex of RAG1 and RAG2 shows that each protein dimerises with itself and each pair then complexes together to from the RAG1-RAG2 V(D)J recombinase enzyme. The different structural elements in RAG1 for UniProtKB:P15919 are: an N-terminal nonamer-binding domain from residues 391-459; a dimerisation and DNA-binding domain from 459-515; an extended pre-RNase H domain from 515-588; the catalytic RNase H domain from 588-719; a ZnC2 domain from 719-791; and ZnH2 domain from 791-962; and a three-helix C-terminal domain from 962-1008 [4,5].", "database": "PfamA", "aliStart": 386, "scoreName": "E-value", "accession": "PF12940.5", "start": 384, "score": 0.0, "identifier": "Recombination-activation protein 1 (RAG1), recombinase", "type": "DBD", "aliEnd": 1021}}, {"startStyle": "straight", "end": 291, "endStyle": "straight", "aliStart": 12, "text": "RAG1_imp_bd", "colour": "#9999ff", "aliEnd": 291, "start": 11, "href": "http://pfam.xfam.org/family/PF12560.6", "type": "pfama", "display": "true", "metadata": {"end": 291, "description": "This region of RAG1 is responsible for binding to importin alpha [1].", "database": "PfamA", "aliStart": 12, "scoreName": "E-value", "accession": "PF12560.6", "start": 11, "score": 1.0999999999999999e-122, "identifier": "RAG1 importin binding", "type": "DBD", "aliEnd": 291}}, {"startStyle": "straight", "end": 383, "endStyle": "straight", "aliStart": 354, "text": "zf-RAG1", "colour": "#9999ff", "aliEnd": 383, "start": 354, "href": "http://pfam.xfam.org/family/PF10426.7", "type": "pfama", "display": "true", "metadata": {"end": 383, "description": "This is a C2-H2 zinc-finger domain closely resembling the classical TFIIIA-type zinc-finger, CX3FX5LX2-3H, despite having a valine and a tyrosine at the core instead of a phenylalanine and a leucine, hence CX3VX1LX2YX2H. The structure, nevertheless, contains the characteristic two-stranded beta-sheet and alpha-helix of a classical zinc-finger. The domain binds one zinc and, in complex with the zinc-RING-finger domain, helps to stabilise the whole of the dimerisation region of recombination activating protein 1 (RAG1) [1]. The function of the whole is to bind double-stranded DNA.", "database": "PfamA", "aliStart": 354, "scoreName": "E-value", "accession": "PF10426.7", "start": 354, "score": 5.899999999999999e-19, "identifier": "Recombination-activating protein 1 zinc-finger domain", "type": "DBD", "aliEnd": 383}}, {"startStyle": "jagged", "end": 916, "endStyle": "jagged", "aliStart": 900, "text": "zf-RAG1", "colour": "#9999ff", "aliEnd": 910, "start": 899, "href": "http://pfam.xfam.org/family/PF10426.7", "type": "pfama", "display": "true", "metadata": {"end": 916, "description": "This is a C2-H2 zinc-finger domain closely resembling the classical TFIIIA-type zinc-finger, CX3FX5LX2-3H, despite having a valine and a tyrosine at the core instead of a phenylalanine and a leucine, hence CX3VX1LX2YX2H. The structure, nevertheless, contains the characteristic two-stranded beta-sheet and alpha-helix of a classical zinc-finger. The domain binds one zinc and, in complex with the zinc-RING-finger domain, helps to stabilise the whole of the dimerisation region of recombination activating protein 1 (RAG1) [1]. The function of the whole is to bind double-stranded DNA.", "database": "PfamA", "aliStart": 900, "scoreName": "E-value", "accession": "PF10426.7", "start": 899, "score": 5.899999999999999e-19, "identifier": "Recombination-activating protein 1 zinc-finger domain", "type": "DBD", "aliEnd": 910}}, {"startStyle": "straight", "end": 331, "endStyle": "straight", "aliStart": 293, "text": "zf-C3HC4", "colour": "#9999ff", "aliEnd": 331, "start": 293, "href": "http://pfam.xfam.org/family/PF00097.23", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid [1]. Many proteins containing a RING finger play a key role in the ubiquitination pathway [2].", "database": "PfamA", "aliStart": 293, "scoreName": "E-value", "accession": "PF00097.23", "start": 293, "score": 1.4e-06, "identifier": "Zinc finger, C3HC4 type (RING finger)", "type": "DBD", "aliEnd": 331}}, {"startStyle": "straight", "end": 331, "endStyle": "straight", "aliStart": 293, "text": "zf-C3HC4_2", "colour": "#9999ff", "aliEnd": 331, "start": 292, "href": "http://pfam.xfam.org/family/PF13923.4", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": NaN, "database": "PfamA", "aliStart": 293, "scoreName": "E-value", "accession": "PF13923.4", "start": 292, "score": 1.7e-06, "identifier": "Zinc finger, C3HC4 type (RING finger)", "type": "DBD", "aliEnd": 331}}, {"startStyle": "straight", "end": 345, "endStyle": "jagged", "aliStart": 289, "text": "zf-RING_6", "colour": "#9999ff", "aliEnd": 339, "start": 286, "href": "http://pfam.xfam.org/family/PF14835.4", "type": "pfama", "display": "true", "metadata": {"end": 345, "description": "The RING domain of the breast and ovarian cancer tumour-suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. A dimer is formed between the RING domains of BRCA1 and BARD1. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level [1]. The corresponding BRCA1-RING domain is on family zf-C3HC4_2, Pfam:PF13923.", "database": "PfamA", "aliStart": 289, "scoreName": "E-value", "accession": "PF14835.4", "start": 286, "score": 0.00054, "identifier": "zf-RING of BARD1-type protein", "type": "DBD", "aliEnd": 339}}, {"startStyle": "straight", "end": 332, "endStyle": "straight", "aliStart": 292, "text": "zf-RING_2", "colour": "#9999ff", "aliEnd": 332, "start": 291, "href": "http://pfam.xfam.org/family/PF13639.4", "type": "pfama", "display": "true", "metadata": {"end": 332, "description": NaN, "database": "PfamA", "aliStart": 292, "scoreName": "E-value", "accession": "PF13639.4", "start": 291, "score": 0.00085, "identifier": "Ring finger domain", "type": "DBD", "aliEnd": 332}}, {"startStyle": "straight", "end": 331, "endStyle": "straight", "aliStart": 293, "text": "zf-C3HC4_4", "colour": "#9999ff", "aliEnd": 331, "start": 293, "href": "http://pfam.xfam.org/family/PF15227.4", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": "This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development [1]. This domain is likely to be DNA-binding [2]. This zinc-finger domain together with the RDM domain, Pfam:PF11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme [3].", "database": "PfamA", "aliStart": 293, "scoreName": "E-value", "accession": "PF15227.4", "start": 293, "score": 0.0018, "identifier": "zinc finger of C3HC4-type, RING", "type": "DBD", "aliEnd": 331}}, {"startStyle": "straight", "end": 347, "endStyle": "jagged", "aliStart": 291, "text": "zf-RING_10", "colour": "#9999ff", "aliEnd": 332, "start": 291, "href": "http://pfam.xfam.org/family/PF16685.3", "type": "pfama", "display": "true", "metadata": {"end": 347, "description": "zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase msl-2 proteins. The domain binds MSL1 and exhibits ubiquitin E3 ligase activity towards H2B K34, the histone proteins [1].", "database": "PfamA", "aliStart": 291, "scoreName": "E-value", "accession": "PF16685.3", "start": 291, "score": 0.0043, "identifier": "zinc RING finger of MSL2", "type": "DBD", "aliEnd": 332}}, {"startStyle": "straight", "end": 329, "endStyle": "straight", "aliStart": 293, "text": "zf-RING_UBOX", "colour": "#9999ff", "aliEnd": 329, "start": 293, "href": "http://pfam.xfam.org/family/PF13445.4", "type": "pfama", "display": "true", "metadata": {"end": 329, "description": "This zinc-finger is a typical RING-type of plant ubiquitin ligases [1].", "database": "PfamA", "aliStart": 293, "scoreName": "E-value", "accession": "PF13445.4", "start": 293, "score": 0.0083, "identifier": "RING-type zinc-finger", "type": "DBD", "aliEnd": 329}}], "length": 1044}