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Conserved domains on  [gi|291409553|ref|XP_002721056|]
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metastasis-associated protein MTA2 [Oryctolagus cuniculus]

Protein Classification

metastasis-associated protein MTA( domain architecture ID 12939588)

metastasis-associated protein MTA similar to human metastasis-associated protein MTA1, a transcriptional coregulator which can act as both a transcriptional corepressor and coactivator, and as part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA

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 ...
 3-168 4.77e-94

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: 287.37  E-value: 4.77e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   3 ANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEesKQPGVSEQQRHQ 82
Cdd:cd04709    1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEE--KSDDLTPKQRHQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553  83 LKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLA 162
Cdd:cd04709   79 LRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPDLQP 158


                 ....*.
gi 291409553 163 EGESDN 168
Cdd:cd04709  159 FPSPDG 164
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 449-524 3.10e-32

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: 119.24  E-value: 3.10e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291409553  449 KNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDL 524
Cdd:pfam17226   3 KTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKPKVRGPLTSIANRL 78
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 267-312 6.91e-26

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: 100.38  E-value: 6.91e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291409553 267 EWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKT 312
Cdd:cd11661    1 EWSESEAKLFEEGLRKYGKDFHDIRQDFLPWKSVGELVEFYYMWKK 46
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 147-198 6.54e-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: 80.73  E-value: 6.54e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291409553  147 IRVGCKYQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVAR 198
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
363-413 1.13e-16

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


:

Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 74.38  E-value: 1.13e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 291409553   363 KGLTCESCHTTQSAQWYAWGPPNmqCRLCASCWIYWKKYGGLKTPTQLEGA 413
Cdd:smart00401   2 SGRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
 
Name Accession Description Interval E-value
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 3-168 4.77e-94

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: 287.37  E-value: 4.77e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   3 ANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEesKQPGVSEQQRHQ 82
Cdd:cd04709    1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEE--KSDDLTPKQRHQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553  83 LKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLA 162
Cdd:cd04709   79 LRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPDLQP 158


                 ....*.
gi 291409553 163 EGESDN 168
Cdd:cd04709  159 FPSPDG 164
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 449-524 3.10e-32

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: 119.24  E-value: 3.10e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291409553  449 KNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDL 524
Cdd:pfam17226   3 KTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKPKVRGPLTSIANRL 78
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 267-312 6.91e-26

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: 100.38  E-value: 6.91e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291409553 267 EWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKT 312
Cdd:cd11661    1 EWSESEAKLFEEGLRKYGKDFHDIRQDFLPWKSVGELVEFYYMWKK 46
BAH smart00439
Bromo adjacent homology domain;
5-140 1.15e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 90.81  E-value: 1.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553     5 MYRVGDYVYFENSSSN-PYLVRRIEELNKTANGN--VEAKVVCLFRRRDISSSLNSLADSNarefeeeskqpgvseqqrh 81
Cdd:smart00439   1 TISVGDFVLVEPDDADePYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKN------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291409553    82 qlkhrELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK--EDCFFYSLVFDPVQKTL 140
Cdd:smart00439  62 -----EVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSF 117
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 4-143 2.06e-21

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: 90.06  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553    4 NMYRVGDYVYFEN-SSSNPYLVRRIEELNKTANGNVEAKVVCLFRRrdissslnsladsnareFEEeskqpgVSEQQRHQ 82
Cdd:pfam01426   1 ETYSVGDFVLVEPdDADEPYYVARIEELFEDTKNGKKMVRVQWFYR-----------------PEE------TVHRAGKA 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291409553   83 LKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK-EDCFFYSLVFDPVQKTLLAD 143
Cdd:pfam01426  58 FNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKePDDFFCELLYDPKTKSFKKL 119
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 147-198 6.54e-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: 80.73  E-value: 6.54e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291409553  147 IRVGCKYQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVAR 198
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
363-413 1.13e-16

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


Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 74.38  E-value: 1.13e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 291409553   363 KGLTCESCHTTQSAQWYAWGPPNmqCRLCASCWIYWKKYGGLKTPTQLEGA 413
Cdd:smart00401   2 SGRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
GATA pfam00320
GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This ...
 367-404 7.32e-13

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: 63.11  E-value: 7.32e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 291409553  367 CESCHTTQSAQWYAWgpPNMQCRLCASCWIYWKKYGGL 404
Cdd:pfam00320   1 CSNCGTTKTPLWRRG--PNGNRTLCNACGLYYKKKGLK 36
ZnF_GATA cd00202
Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] ...
 366-421 2.76e-11

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: 58.92  E-value: 2.76e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291409553 366 TCESCHTTQSAQWYAWgpPNMQCRLCASCWIYWKKYgGLKTPTQLEGAARGTTEPH 421
Cdd:cd00202    1 ACSNCGTTTTPLWRRG--PSGGSTLCNACGLYWKKH-GVMRPLSKRKKDQIKRRNR 53
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 267-311 2.30e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 44.80  E-value: 2.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 291409553  267 EWSASEAMLFEEALEKYGKDFNDIrQDFLPWKSLASIVQFYYMWK 311
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLGNRWKKI-AKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
266-313 4.04e-05

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 41.44  E-value: 4.04e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 291409553   266 EEWSASEAMLFEEALEKYG-KDFNDIRQdFLPWKSLASIVQFYYMWKTT 313
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGkNNWEKIAK-ELPGRTAEQCRERWRNLLKP 49
 
Name Accession Description Interval E-value
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 3-168 4.77e-94

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: 287.37  E-value: 4.77e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   3 ANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEesKQPGVSEQQRHQ 82
Cdd:cd04709    1 ANMYRVGDYVYFESSPNNPYLIRRIEELNKTARGHVEAKVVCYYRRRDIPDSLYQLADQHRRELEE--KSDDLTPKQRHQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553  83 LKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLA 162
Cdd:cd04709   79 LRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDTFFYSLVYDPEQKTLLADQGEIRVGPSYQAKLPDLQP 158


                 ....*.
gi 291409553 163 EGESDN 168
Cdd:cd04709  159 FPSPDG 164
MTA_R1 pfam17226
MTA R1 domain; The R1 domain is found in the MTA1 protein and its homologs. The domain is ...
 449-524 3.10e-32

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: 119.24  E-value: 3.10e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291409553  449 KNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDL 524
Cdd:pfam17226   3 KTRQAFYLQTTPLTRLARRLCRDILRPRHAARRPFVPINIAAIKAECQARLPEKSKNPLKLKPKVRGPLTSIANRL 78
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 267-312 6.91e-26

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: 100.38  E-value: 6.91e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291409553 267 EWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKT 312
Cdd:cd11661    1 EWSESEAKLFEEGLRKYGKDFHDIRQDFLPWKSVGELVEFYYMWKK 46
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 3-140 2.53e-23

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: 95.54  E-value: 2.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   3 ANMYRVGDYVYFENSS---SNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSnarefeeeskqpgvseqq 79
Cdd:cd04370    1 GITYEVGDSVYVEPDDsikSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALR------------------ 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291409553  80 rhqlkhRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK--EDCFFYSLVFDPVQKTL 140
Cdd:cd04370   63 ------RELFLSDHLDEIPVESIIGKCKVLFVSEFEGLKQRPNKidTDDFFCRLAYDPTTKEF 119
BAH smart00439
Bromo adjacent homology domain;
5-140 1.15e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 90.81  E-value: 1.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553     5 MYRVGDYVYFENSSSN-PYLVRRIEELNKTANGN--VEAKVVCLFRRRDISSSLNSLADSNarefeeeskqpgvseqqrh 81
Cdd:smart00439   1 TISVGDFVLVEPDDADePYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKN------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291409553    82 qlkhrELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK--EDCFFYSLVFDPVQKTL 140
Cdd:smart00439  62 -----EVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSF 117
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 4-143 2.06e-21

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: 90.06  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553    4 NMYRVGDYVYFEN-SSSNPYLVRRIEELNKTANGNVEAKVVCLFRRrdissslnsladsnareFEEeskqpgVSEQQRHQ 82
Cdd:pfam01426   1 ETYSVGDFVLVEPdDADEPYYVARIEELFEDTKNGKKMVRVQWFYR-----------------PEE------TVHRAGKA 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291409553   83 LKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK-EDCFFYSLVFDPVQKTLLAD 143
Cdd:pfam01426  58 FNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKePDDFFCELLYDPKTKSFKKL 119
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 147-198 6.54e-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: 80.73  E-value: 6.54e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291409553  147 IRVGCKYQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVAR 198
Cdd:pfam01448   1 IRVGPRYQAEIPELLPPSEEEDRYEEEDELLVWDPNHNLPDRKLDEYLVVAR 52
ZnF_GATA smart00401
zinc finger binding to DNA consensus sequence [AT]GATA[AG];
363-413 1.13e-16

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


Pssm-ID: 214648 [Multi-domain]  Cd Length: 52  Bit Score: 74.38  E-value: 1.13e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 291409553   363 KGLTCESCHTTQSAQWYAWGPPNmqCRLCASCWIYWKKYGGLKTPTQLEGA 413
Cdd:smart00401   2 SGRSCSNCGTTETPLWRRGPSGN--KTLCNACGLYYKKHGGLKRPLSLKKD 50
GATA pfam00320
GATA zinc finger; This domain uses four cysteine residues to coordinate a zinc ion. This ...
 367-404 7.32e-13

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: 63.11  E-value: 7.32e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 291409553  367 CESCHTTQSAQWYAWgpPNMQCRLCASCWIYWKKYGGL 404
Cdd:pfam00320   1 CSNCGTTKTPLWRRG--PNGNRTLCNACGLYYKKKGLK 36
ZnF_GATA cd00202
Zinc finger DNA binding domain; binds specifically to DNA consensus sequence [AT]GATA[AG] ...
 366-421 2.76e-11

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: 58.92  E-value: 2.76e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291409553 366 TCESCHTTQSAQWYAWgpPNMQCRLCASCWIYWKKYgGLKTPTQLEGAARGTTEPH 421
Cdd:cd00202    1 ACSNCGTTTTPLWRRG--PSGGSTLCNACGLYWKKH-GVMRPLSKRKKDQIKRRNR 53
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 5-135 1.80e-06

BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. 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: 240061  Cd Length: 135  Bit Score: 47.75  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   5 MYRVGDYVYFENS-SSNPYLVRRIEE-LNKTANGNVEAKVVC-----------LFRRRDISSSLNslADSnarefeeesk 71
Cdd:cd04710   11 LLKVNDHIYMSSEpPGEPYYIGRIMEfVPKHEFPSGIHARVFpasyfqvrlnwYYRPRDISRRVV--ADS---------- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291409553  72 qpgvseqqrhqlkhRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDP 135
Cdd:cd04710   79 --------------RLLYASMHSDICPIGSVRGKCTVRHRDQIPDLEEYKKRPNHFYFDQLFDR 128
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 267-311 2.30e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 44.80  E-value: 2.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 291409553  267 EWSASEAMLFEEALEKYGKDFNDIrQDFLPWKSLASIVQFYYMWK 311
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLGNRWKKI-AKLLPGRTDNQCKNRWQNYL 46
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 267-311 3.54e-05

'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.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 41.41  E-value: 3.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291409553 267 EWSASEAMLFEEALEKYG-KDFNDIRQdFLPWKSLASIVQFYYMWK 311
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGkNNWEKIAK-ELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
266-313 4.04e-05

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 41.44  E-value: 4.04e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 291409553   266 EEWSASEAMLFEEALEKYG-KDFNDIRQdFLPWKSLASIVQFYYMWKTT 313
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGkNNWEKIAK-ELPGRTAEQCRERWRNLLKP 49
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 7-135 1.90e-03

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: 38.54  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291409553   7 RVGDYVYFENSSSN--PYlVRRIEELNKTANGNVEAKVVCLFRrrdissslnsladsnarefEEESKQpgvSEQQRHQLK 84
Cdd:cd04714    5 RVGDCVLFKSPGRPslPY-VARIESLWEDPEGNMVVRVKWYYR-------------------PEETKG---GRKPNHGEK 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 291409553  85 hrELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEK----EDCFFYSLVFDP 135
Cdd:cd04714   62 --ELFASDHQDENSVQTIEHKCYVLTFAEYERLARVKKKpqdgVDFYYCAGTYNP 114
 
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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