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Conserved domains on  [gi|1985665609|emb|CAE6133191|]
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unnamed protein product [Arabidopsis arenosa]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 111-257 2.18e-88

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: 271.26  E-value: 2.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 111 TGKGKGKRTHFKQFAYDGNTYDLEDPVLLVPEDKsQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRGGGNWQSSDT 190
Cdd:cd04713     1 TGKGKKKKCHYTSFEKDGNKYRLEDCVLLVPEDD-QKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKKGGNWKAEDP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609 191 RELFYSFHRDEVPAESVMHRCVVYFVPAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLTDKDYEDSKQ 257
Cdd:cd04713    80 RELFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKGHSGFIVRRVYDNVNKKLWKLTDQDYEDERQ 146
TFS2M super family cl46921
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
342-475 2.44e-19

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


The actual alignment was detected with superfamily member smart00510:

Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 83.52  E-value: 2.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609  342 DAHRDKCLGKLLEAVHHICYIPEnkqagdeakvgsdgshleqdgkntkpengkdeKFLWPDAAVPPVCALENAShasLAS 421
Cdd:smart00510   1 DKVRDKCQEMLYKALQKISDPEE--------------------------------IELDPTELAVQIEAEMFSE---FGT 45

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609  422 DFQKYNQKMRTLVFNLK--NTALLARRLLNGELEPAKILNMSPTEL-KEGLTADETT 475
Cdd:smart00510  46 TDKKYKNKYRSLYFNLKdkKNPDLRRKVLNGEITPEKLATMTAEELaSAELKEKREK 102
 
Name Accession Description Interval E-value
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 111-257 2.18e-88

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: 271.26  E-value: 2.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 111 TGKGKGKRTHFKQFAYDGNTYDLEDPVLLVPEDKsQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRGGGNWQSSDT 190
Cdd:cd04713     1 TGKGKKKKCHYTSFEKDGNKYRLEDCVLLVPEDD-QKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKKGGNWKAEDP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609 191 RELFYSFHRDEVPAESVMHRCVVYFVPAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLTDKDYEDSKQ 257
Cdd:cd04713    80 RELFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKGHSGFIVRRVYDNVNKKLWKLTDQDYEDERQ 146
BAH smart00439
Bromo adjacent homology domain;
130-248 1.81e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 90.04  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609  130 TYDLEDPVLLVPEDKSQKPYVAIIKDITQTKDGS--MMILGQWFYRPEEAEKrggGNWQSSDTRELFYSFHRDEVPAESV 207
Cdd:smart00439   1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVL---EKAALFDKNEVFLSDEYDTVPLSDI 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1985665609  208 MHRCVVYFVPA---HKQLPKRKNNPGFIVRKVYDTVEKKLWKLT 248
Cdd:smart00439  78 IGKCNVLYKSDypgLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 129-248 8.06e-20

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: 85.44  E-value: 8.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 129 NTYDLEDPVLLVPEDKSQKPYVAIIKDI-TQTKDGSMMILGQWFYRPEEAEKRGGGnwqSSDTRELFYSFHRDEVPAESV 207
Cdd:pfam01426   1 ETYSVGDFVLVEPDDADEPYYVARIEELfEDTKNGKKMVRVQWFYRPEETVHRAGK---AFNKDELFLSDEEDDVPLSAI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1985665609 208 MHRCVVYFV--PAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLT 248
Cdd:pfam01426  78 IGKCSVLHKsdLESLDPYKIKEPDDFFCELLYDPKTKSFKKLP 120
TFS2M smart00510
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
342-475 2.44e-19

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 83.52  E-value: 2.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609  342 DAHRDKCLGKLLEAVHHICYIPEnkqagdeakvgsdgshleqdgkntkpengkdeKFLWPDAAVPPVCALENAShasLAS 421
Cdd:smart00510   1 DKVRDKCQEMLYKALQKISDPEE--------------------------------IELDPTELAVQIEAEMFSE---FGT 45

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609  422 DFQKYNQKMRTLVFNLK--NTALLARRLLNGELEPAKILNMSPTEL-KEGLTADETT 475
Cdd:smart00510  46 TDKKYKNKYRSLYFNLKdkKNPDLRRKVLNGEITPEKLATMTAEELaSAELKEKREK 102
TFIIS_M pfam07500
Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase ...
 340-485 5.48e-17

Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III), this domain and pfam01096 are required for transcription activity.


Pssm-ID: 462184  Cd Length: 112  Bit Score: 76.86  E-value: 5.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 340 TGDAHRDKCLGKLLEAVHHICYIPENKQAGDEAKvgsdgshleqdgkntkpengkdekflwpdaavppvcALENASHASL 419
Cdd:pfam07500   1 TGDKVRDKCRELLYDALAKDSTEASEEDALELAV------------------------------------EIEEALFKKF 44

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985665609 420 ASDFQKYNQKMRTLVFNLK--NTALLARRLLNGELEPAKILNMSPTELKEGLTADETTKKEPDDADRM 485
Cdd:pfam07500  45 GGTNKKYKNKIRSLLFNLKdkKNPDLRRRVLSGEISPEKLVTMSPEEMASEELKKEREKIEKEALKEA 112
TFSII TIGR01385
transcription elongation factor S-II; This model represents eukaryotic transcription ...
 425-525 8.32e-03

transcription elongation factor S-II; This model represents eukaryotic transcription elongation factor S-II. This protein allows stalled RNA transcription complexes to perform a cleavage of the nascent RNA and restart at the newly generated 3-prime end.


Pssm-ID: 273592 [Multi-domain]  Cd Length: 299  Bit Score: 38.67  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 425 KYNQKMRTLVFNL--KNTALLARRLLNGELEPAKILNMS-----PTELKEglTADETTKKEPDDADR--MQMTSV---RC 492
Cdd:TIGR01385 184 AYKARYRSIYSNLrdKNNPDLRHNVLTGEITPEKLATMTaeemaSAELKQ--EREEITKENLFEAQGakIQKAVTdlfTC 261

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1985665609 493 SRCNQLKVGLRDViQAGHGDRYQ---LECVDCGYSW 525
Cdd:TIGR01385 262 GKCKQKKCTYYQL-QTRSADEPMttfVTCEECGNRW 296
 
Name Accession Description Interval E-value
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 111-257 2.18e-88

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: 271.26  E-value: 2.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 111 TGKGKGKRTHFKQFAYDGNTYDLEDPVLLVPEDKsQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRGGGNWQSSDT 190
Cdd:cd04713     1 TGKGKKKKCHYTSFEKDGNKYRLEDCVLLVPEDD-QKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKKGGNWKAEDP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609 191 RELFYSFHRDEVPAESVMHRCVVYFVPAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLTDKDYEDSKQ 257
Cdd:cd04713    80 RELFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKGHSGFIVRRVYDNVNKKLWKLTDQDYEDERQ 146
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 128-248 1.79e-22

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: 93.23  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 128 GNTYDLEDPVLLVPED--KSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKrggGNWQSSDTRELFYSFHRDEVPAE 205
Cdd:cd04370     1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPK---GLSPFALRRELFLSDHLDEIPVE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1985665609 206 SVMHRCVVYFVP---AHKQLPKRKNNPGFIVRKVYDTVEKKLWKLT 248
Cdd:cd04370    78 SIIGKCKVLFVSefeGLKQRPNKIDTDDFFCRLAYDPTTKEFKALE 123
BAH smart00439
Bromo adjacent homology domain;
130-248 1.81e-21

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 90.04  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609  130 TYDLEDPVLLVPEDKSQKPYVAIIKDITQTKDGS--MMILGQWFYRPEEAEKrggGNWQSSDTRELFYSFHRDEVPAESV 207
Cdd:smart00439   1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVL---EKAALFDKNEVFLSDEYDTVPLSDI 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1985665609  208 MHRCVVYFVPA---HKQLPKRKNNPGFIVRKVYDTVEKKLWKLT 248
Cdd:smart00439  78 IGKCNVLYKSDypgLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 129-248 8.06e-20

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: 85.44  E-value: 8.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 129 NTYDLEDPVLLVPEDKSQKPYVAIIKDI-TQTKDGSMMILGQWFYRPEEAEKRGGGnwqSSDTRELFYSFHRDEVPAESV 207
Cdd:pfam01426   1 ETYSVGDFVLVEPDDADEPYYVARIEELfEDTKNGKKMVRVQWFYRPEETVHRAGK---AFNKDELFLSDEEDDVPLSAI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1985665609 208 MHRCVVYFV--PAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLT 248
Cdd:pfam01426  78 IGKCSVLHKsdLESLDPYKIKEPDDFFCELLYDPKTKSFKKLP 120
TFS2M smart00510
Domain in the central regions of transcription elongation factor S-II (and elsewhere);
342-475 2.44e-19

Domain in the central regions of transcription elongation factor S-II (and elsewhere);


Pssm-ID: 128786 [Multi-domain]  Cd Length: 102  Bit Score: 83.52  E-value: 2.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609  342 DAHRDKCLGKLLEAVHHICYIPEnkqagdeakvgsdgshleqdgkntkpengkdeKFLWPDAAVPPVCALENAShasLAS 421
Cdd:smart00510   1 DKVRDKCQEMLYKALQKISDPEE--------------------------------IELDPTELAVQIEAEMFSE---FGT 45

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985665609  422 DFQKYNQKMRTLVFNLK--NTALLARRLLNGELEPAKILNMSPTEL-KEGLTADETT 475
Cdd:smart00510  46 TDKKYKNKYRSLYFNLKdkKNPDLRRKVLNGEITPEKLATMTAEELaSAELKEKREK 102
TFIIS_M pfam07500
Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase ...
 340-485 5.48e-17

Transcription factor S-II (TFIIS), central domain; Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III), this domain and pfam01096 are required for transcription activity.


Pssm-ID: 462184  Cd Length: 112  Bit Score: 76.86  E-value: 5.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 340 TGDAHRDKCLGKLLEAVHHICYIPENKQAGDEAKvgsdgshleqdgkntkpengkdekflwpdaavppvcALENASHASL 419
Cdd:pfam07500   1 TGDKVRDKCRELLYDALAKDSTEASEEDALELAV------------------------------------EIEEALFKKF 44

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985665609 420 ASDFQKYNQKMRTLVFNLK--NTALLARRLLNGELEPAKILNMSPTELKEGLTADETTKKEPDDADRM 485
Cdd:pfam07500  45 GGTNKKYKNKIRSLLFNLKdkKNPDLRRRVLSGEISPEKLVTMSPEEMASEELKKEREKIEKEALKEA 112
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 135-229 1.04e-14

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: 70.89  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 135 DPVLLVPEDKSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEkrgGGNWQSSDTRELFYSFHRDEVPAESVMHRCVVY 214
Cdd:cd04714     8 DCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETK---GGRKPNHGEKELFASDHQDENSVQTIEHKCYVL 84

                          90
                  ....*....|....*
gi 1985665609 215 FVPAHKQLPKRKNNP 229
Cdd:cd04714    85 TFAEYERLARVKKKP 99
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 128-247 9.36e-08

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: 51.05  E-value: 9.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 128 GNTYDLEDPVLLVPEDKSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRgggnwqssDTR-----ELFYSFHRDEV 202
Cdd:cd04717     1 GLQYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHE--------PTRkfyknEVFKSPLYETV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1985665609 203 PAESVMHRCVVYFVPAH-KQLPKR-KNNPGFIVRKVYDTVEKKLWKL 247
Cdd:cd04717    73 PVEEIVGKCAVMDVKDYiKGRPTEiSEEDVYVCESRYNESAKSFKKI 119
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 124-207 1.62e-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: 240072  Cd Length: 130  Bit Score: 47.82  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 124 FAYDGNTYDLEDPVLLVPEDKSQkpYVAIIKDITQTKDGSMMILGQWFYRPEEAekrggGNWQSSDT---RELFYSFHRD 200
Cdd:cd04721     1 FCRNGVTISVHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWFHTTDEV-----GAALSPDSvnpREIFLSPNLQ 73


                  ....*..
gi 1985665609 201 EVPAESV 207
Cdd:cd04721    74 VISVECI 80
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 128-228 1.51e-03

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: 38.96  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 128 GNTYDLEDPVLlVPEDKSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEA--EKRGggnwQSSDTRELFYSFHRDEVPAE 205
Cdd:cd04716     1 GITYNLGDDAY-VQGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDTviERQA----TNHDKKRVFYSEIKNDNPLD 75

                          90       100
                  ....*....|....*....|...
gi 1985665609 206 SVMHRCVVYFVPAHKQLPKRKNN 228
Cdd:cd04716    76 CLISKVKILQVPPNVGTKRKKPN 98
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
 158-245 2.07e-03

BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) 1. 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: 240063  Cd Length: 130  Bit Score: 38.54  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 158 QTKDGSMMILGQWFYRPeeaekrgggnwqsSDT--------RELFYSFHRDEVPAESVMHRCV-VYFVPAHKQlPKRKNN 228
Cdd:cd04712    43 KGSDGSKMFHGRWLYRG-------------CDTvlgnyaneRELFLTNECTCLELDLLSTEIKgVHKVDWSGT-PWGKGL 108

                          90
                  ....*....|....*..
gi 1985665609 229 PGFIVRKVYDTVEKKLW 245
Cdd:cd04712   109 PEFFVRQSYYWPERGAF 125
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 127-213 4.26e-03

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: 37.74  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 127 DGNTYDLEDPVLLVPEDKSQKPYVAIIKDITQTKDGSMMILGQ------------WFYRPEEAEKRgggnwQSSDTRELF 194
Cdd:cd04710     8 NGELLKVNDHIYMSSEPPGEPYYIGRIMEFVPKHEFPSGIHARvfpasyfqvrlnWYYRPRDISRR-----VVADSRLLY 82

                          90
                  ....*....|....*....
gi 1985665609 195 YSFHRDEVPAESVMHRCVV 213
Cdd:cd04710    83 ASMHSDICPIGSVRGKCTV 101
TFSII TIGR01385
transcription elongation factor S-II; This model represents eukaryotic transcription ...
 425-525 8.32e-03

transcription elongation factor S-II; This model represents eukaryotic transcription elongation factor S-II. This protein allows stalled RNA transcription complexes to perform a cleavage of the nascent RNA and restart at the newly generated 3-prime end.


Pssm-ID: 273592 [Multi-domain]  Cd Length: 299  Bit Score: 38.67  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985665609 425 KYNQKMRTLVFNL--KNTALLARRLLNGELEPAKILNMS-----PTELKEglTADETTKKEPDDADR--MQMTSV---RC 492
Cdd:TIGR01385 184 AYKARYRSIYSNLrdKNNPDLRHNVLTGEITPEKLATMTaeemaSAELKQ--EREEITKENLFEAQGakIQKAVTdlfTC 261

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1985665609 493 SRCNQLKVGLRDViQAGHGDRYQ---LECVDCGYSW 525
Cdd:TIGR01385 262 GKCKQKKCTYYQL-QTRSADEPMttfVTCEECGNRW 296
 
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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