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Conserved domains on  [gi|1060098977|ref|NP_001317373|]
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metastasis-associated protein MTA3 isoform e [Homo sapiens]

Protein Classification

BAH_MTA and MTA_R1 domain-containing protein( domain architecture ID 12939604)

protein containing domains BAH_MTA, ELM2, ZnF_GATA, and MTA_R1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 3-170 1.42e-97

BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. 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: 240060  Cd Length: 164  Bit Score: 292.37  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   3 ANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKEIEEESEttveaDLTDKQ 82
Cdd:cd04709     1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEEKSD-----DLTPKQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977  83 KHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPE 162
Cdd:cd04709    76 RHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPD 155


                  ....*...
gi 1060098977 163 MLLEGESD 170
Cdd:cd04709   156 LQPFPSPD 163
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 397-473 9.30e-35

MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is composed of 4 alpha helices. It has been shown to bind to the RBBP4 protein. The MTA proteins contain a second partial copy of this domain called R2. The R2 domain is matched by this model for some proteins.


:

Pssm-ID: 465388  Cd Length: 78  Bit Score: 125.40  E-value: 9.30e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977 397 AVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSK-STRKPLACIIGYL 473
Cdd:pfam17226   1 AMKTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKpKVRGPLTSIANRL 78
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 150-201 1.18e-19

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


:

Pssm-ID: 460214  Cd Length: 53  Bit Score: 82.28  E-value: 1.18e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1060098977 150 IRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVAR 201
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
312-361 1.42e-14

zinc finger binding to DNA consensus sequence [AT]GATA[AG];


:

Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 67.83  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1060098977  312 GRACESCYATQSHQWYSWGPPNmqCRLCAICWLYWKKYGGLKMPTQSEEE 361
Cdd:smart00401   3 GRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
SANT super family cl21498
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 234-252 5.87e-06

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


The actual alignment was detected with superfamily member cd11661:

Pssm-ID: 473887 [Multi-domain]  Cd Length: 46  Bit Score: 43.37  E-value: 5.87e-06
                          10
                  ....*....|....*....
gi 1060098977 234 LLPWKSLTSIIEYYYMWKT 252
Cdd:cd11661    28 FLPWKSVGELVEFYYMWKK 46
 
Name Accession Description Interval E-value
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 3-170 1.42e-97

BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. 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: 240060  Cd Length: 164  Bit Score: 292.37  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   3 ANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKEIEEESEttveaDLTDKQ 82
Cdd:cd04709     1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEEKSD-----DLTPKQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977  83 KHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPE 162
Cdd:cd04709    76 RHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPD 155


                  ....*...
gi 1060098977 163 MLLEGESD 170
Cdd:cd04709   156 LQPFPSPD 163
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 397-473 9.30e-35

MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is composed of 4 alpha helices. It has been shown to bind to the RBBP4 protein. The MTA proteins contain a second partial copy of this domain called R2. The R2 domain is matched by this model for some proteins.


Pssm-ID: 465388  Cd Length: 78  Bit Score: 125.40  E-value: 9.30e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977 397 AVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSK-STRKPLACIIGYL 473
Cdd:pfam17226   1 AMKTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKpKVRGPLTSIANRL 78
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 4-147 8.95e-24

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: 96.22  E-value: 8.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   4 NMYRVGDYVYFEN-SSSNPYLIRRIEELnKTASGNVEAKV-VC-FYRRRDISNTLimladkhakeieeesettveadltd 80
Cdd:pfam01426   1 ETYSVGDFVLVEPdDADEPYYVARIEEL-FEDTKNGKKMVrVQwFYRPEETVHRA------------------------- 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977  81 kqKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYL-DKEDTFFYSLVYDPSLKTLLADK 147
Cdd:pfam01426  55 --GKAFNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKiKEPDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
5-147 7.31e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 88.12  E-value: 7.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977    5 MYRVGDYVYFENSSSN-PYLIRRIEELNKTASGN--VEAKVVCFYRRRDIsntlimladkhakeIEEEsettveADLTDK 81
Cdd:smart00439   1 TISVGDFVLVEPDDADePYYIGRIEEIFETKKNSesKMVRVRWFYRPEET--------------VLEK------AALFDK 60

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977   82 qkhqlkhRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDK--EDTFFYSLVYDPSLKTLLADK 147
Cdd:smart00439  61 -------NEVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKKLP 121
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 150-201 1.18e-19

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 82.28  E-value: 1.18e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1060098977 150 IRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVAR 201
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
312-361 1.42e-14

zinc finger binding to DNA consensus sequence [AT]GATA[AG];


Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 67.83  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1060098977  312 GRACESCYATQSHQWYSWGPPNmqCRLCAICWLYWKKYGGLKMPTQSEEE 361
Cdd:smart00401   3 GRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
GATA pfam00320
GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This ...
 315-352 1.25e-10

GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This domain binds to DNA. Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contain a single copy of the domain.


Pssm-ID: 425605 [Multi-domain]  Cd Length: 36  Bit Score: 56.17  E-value: 1.25e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1060098977 315 CESCYATQSHQWYSWgpPNMQCRLCAICWLYWKKYGGL 352
Cdd:pfam00320   1 CSNCGTTKTPLWRRG--PNGNRTLCNACGLYYKKKGLK 36
ZnF_GATA cd00202
Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] ...
 314-362 4.52e-10

Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] promoter elements; a subset of family members may also bind protein; zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C


Pssm-ID: 238123 [Multi-domain]  Cd Length: 54  Bit Score: 55.07  E-value: 4.52e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1060098977 314 ACESCYATQSHQWYSWgpPNMQCRLCAICWLYWKKYgGLKMPTQSEEEK 362
Cdd:cd00202     1 ACSNCGTTTTPLWRRG--PSGGSTLCNACGLYWKKH-GVMRPLSKRKKD 46
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 234-252 5.87e-06

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 43.37  E-value: 5.87e-06
                          10
                  ....*....|....*....
gi 1060098977 234 LLPWKSLTSIIEYYYMWKT 252
Cdd:cd11661    28 FLPWKSVGELVEFYYMWKK 46
 
Name Accession Description Interval E-value
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 3-170 1.42e-97

BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. 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: 240060  Cd Length: 164  Bit Score: 292.37  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   3 ANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKEIEEESEttveaDLTDKQ 82
Cdd:cd04709     1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEEKSD-----DLTPKQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977  83 KHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPE 162
Cdd:cd04709    76 RHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPD 155


                  ....*...
gi 1060098977 163 MLLEGESD 170
Cdd:cd04709   156 LQPFPSPD 163
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 397-473 9.30e-35

MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is composed of 4 alpha helices. It has been shown to bind to the RBBP4 protein. The MTA proteins contain a second partial copy of this domain called R2. The R2 domain is matched by this model for some proteins.


Pssm-ID: 465388  Cd Length: 78  Bit Score: 125.40  E-value: 9.30e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977 397 AVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSK-STRKPLACIIGYL 473
Cdd:pfam17226   1 AMKTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKpKVRGPLTSIANRL 78
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 3-143 3.68e-24

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: 97.46  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   3 ANMYRVGDYVYFENSS---SNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNtlimladkhakeieeesettveadlt 79
Cdd:cd04370     1 GITYEVGDSVYVEPDDsikSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPK-------------------------- 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1060098977  80 DKQKHQLKhRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDK--EDTFFYSLVYDPSLKTL 143
Cdd:cd04370    55 GLSPFALR-RELFLSDHLDEIPVESIIGKCKVLFVSEFEGLKQRPNKidTDDFFCRLAYDPTTKEF 119
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 4-147 8.95e-24

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: 96.22  E-value: 8.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977   4 NMYRVGDYVYFEN-SSSNPYLIRRIEELnKTASGNVEAKV-VC-FYRRRDISNTLimladkhakeieeesettveadltd 80
Cdd:pfam01426   1 ETYSVGDFVLVEPdDADEPYYVARIEEL-FEDTKNGKKMVrVQwFYRPEETVHRA------------------------- 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977  81 kqKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYL-DKEDTFFYSLVYDPSLKTLLADK 147
Cdd:pfam01426  55 --GKAFNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKiKEPDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
5-147 7.31e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 88.12  E-value: 7.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098977    5 MYRVGDYVYFENSSSN-PYLIRRIEELNKTASGN--VEAKVVCFYRRRDIsntlimladkhakeIEEEsettveADLTDK 81
Cdd:smart00439   1 TISVGDFVLVEPDDADePYYIGRIEEIFETKKNSesKMVRVRWFYRPEET--------------VLEK------AALFDK 60

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060098977   82 qkhqlkhRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDK--EDTFFYSLVYDPSLKTLLADK 147
Cdd:smart00439  61 -------NEVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKKLP 121
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 150-201 1.18e-19

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 82.28  E-value: 1.18e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1060098977 150 IRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVAR 201
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
312-361 1.42e-14

zinc finger binding to DNA consensus sequence [AT]GATA[AG];


Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 67.83  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1060098977  312 GRACESCYATQSHQWYSWGPPNmqCRLCAICWLYWKKYGGLKMPTQSEEE 361
Cdd:smart00401   3 GRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
GATA pfam00320
GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This ...
 315-352 1.25e-10

GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This domain binds to DNA. Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contain a single copy of the domain.


Pssm-ID: 425605 [Multi-domain]  Cd Length: 36  Bit Score: 56.17  E-value: 1.25e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1060098977 315 CESCYATQSHQWYSWgpPNMQCRLCAICWLYWKKYGGL 352
Cdd:pfam00320   1 CSNCGTTKTPLWRRG--PNGNRTLCNACGLYYKKKGLK 36
ZnF_GATA cd00202
Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] ...
 314-362 4.52e-10

Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] promoter elements; a subset of family members may also bind protein; zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C


Pssm-ID: 238123 [Multi-domain]  Cd Length: 54  Bit Score: 55.07  E-value: 4.52e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1060098977 314 ACESCYATQSHQWYSWgpPNMQCRLCAICWLYWKKYgGLKMPTQSEEEK 362
Cdd:cd00202     1 ACSNCGTTTTPLWRRG--PSGGSTLCNACGLYWKKH-GVMRPLSKRKKD 46
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 234-252 5.87e-06

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 43.37  E-value: 5.87e-06
                          10
                  ....*....|....*....
gi 1060098977 234 LLPWKSLTSIIEYYYMWKT 252
Cdd:cd11661    28 FLPWKSVGELVEFYYMWKK 46
 
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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