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Conserved domains on  [gi|1720398740|ref|XP_030106223|]
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bromo adjacent homology domain-containing 1 protein isoform X4 [Mus musculus]

Protein Classification

BAH_BAHCC1 domain-containing protein( domain architecture ID 10140545)

BAH_BAHCC1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
615-725 2.93e-52

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: 177.21  E-value: 2.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPRKtSTPYVAKISALWENPEsGELMMSLLWYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVA 694
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRP-SLPYVARIESLWEDPE-GNMVVRVKWYYRPEETKGGRKPNHGE---KELFASDHQDENSVQ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720398740 695 CIEEKCYVLTFAEY---------------CRFCAMAKRRGEGLPSR 725
Cdd:cd04714    76 TIEHKCYVLTFAEYerlarvkkkpqdgvdFYYCAGTYNPDTGMLKC 121
PHA03247 super family cl33720
large tegument protein UL36; Provisional
149-369 2.20e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  149 GDPHRSRDRATGSWSFSKKRPRLGDLGEGSRDLSPELAPDEGARRDG----DPAPKRLASLNAAAFLKLSQERELPL-RP 223
Cdd:PHA03247  2752 GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpspwDPADPPAAVLAPAAALPPAASPAGPLpPP 2831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  224 SRAQAEADGRSTEPLAPRILRPKVNGKNCPKARQGAgSGEATGPPNWQEQPNERWPSAPPHGPPTQPSHQAPgkalENPL 303
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP-SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPE 2906
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398740  304 RPNLPllmggQAALKPEPGRPGEESPAPKQELHQPSFPAPQLSPLPMPGNPADYSGPCGGPELTAL 369
Cdd:PHA03247  2907 RPPQP-----QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
279-563 5.11e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  279 PSAPPHGPPTQPSHQAPGKALENPLRPNLPLLMGGQAALKPEPGRPGEESPAPKQELHQPSFPAP--------QLSPLPM 350
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPspapdlseMLRPVGS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  351 PGNPADYSGPCGGPELTALGSFYLYCGQDGLqcgaysPCPMLPEGKLSPVAAPNE-GLLMAPSSVPSGVPFQHPPWSAPR 429
Cdd:PHA03307   144 PGPPPAASPPAAGASPAAVASDAASSRQAAL------PLSSPEETARAPSSPPAEpPPSTPPAAASPRPPRRSSPISASA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  430 YCSSEDTGANGYSICGVLPLSLTHI--------GTTCGGCPYKMPFTAEGCR---SLGQLEFPLPEAGHPASPAHPLLGC 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSessgcgwgPENECPLPRPAPITLPTRIweaSGWNGPSSRPGPASSSSSPRERSPS 297
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398740  499 PVPSVP--PAAEPIPHLQTPISEPQTVARACPQSAKPPSGSKSGLRTGSSCRHAV--RSKAARRPSHPK 563
Cdd:PHA03307   298 PSPSSPgsGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpsRPPPPADPSSPR 366
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
615-725 2.93e-52

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: 177.21  E-value: 2.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPRKtSTPYVAKISALWENPEsGELMMSLLWYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVA 694
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRP-SLPYVARIESLWEDPE-GNMVVRVKWYYRPEETKGGRKPNHGE---KELFASDHQDENSVQ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720398740 695 CIEEKCYVLTFAEY---------------CRFCAMAKRRGEGLPSR 725
Cdd:cd04714    76 TIEHKCYVLTFAEYerlarvkkkpqdgvdFYYCAGTYNPDTGMLKC 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
616-732 2.19e-16

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: 75.81  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 616 ETIRVRDTVLLKSGPrKTSTPYVAKISALWENPESGELMMSLLWYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVAC 695
Cdd:pfam01426   1 ETYSVGDFVLVEPDD-ADEPYYVARIEELFEDTKNGKKMVRVQWFYRPEETVHRAGKAFNK---DELFLSDEEDDVPLSA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720398740 696 IEEKCYVLTFAEYCRFCAMAKRRGEGL-------PSRKTALVPP 732
Cdd:pfam01426  77 IIGKCSVLHKSDLESLDPYKIKEPDDFfcellydPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
617-720 1.37e-15

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 73.48  E-value: 1.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  617 TIRVRDTVLLKSgPRKTSTPYVAKISALWENPESGELMMSLL-WYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVAC 695
Cdd:smart00439   1 TISVGDFVLVEP-DDADEPYYIGRIEEIFETKKNSESKMVRVrWFYRPEETVLEKAALFDK---NEVFLSDEYDTVPLSD 76
                           90       100
                   ....*....|....*....|....*
gi 1720398740  696 IEEKCYVLTFAEYCRFCAMAKRRGE 720
Cdd:smart00439  77 IIGKCNVLYKSDYPGLRPEGSIGEP 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
149-369 2.20e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  149 GDPHRSRDRATGSWSFSKKRPRLGDLGEGSRDLSPELAPDEGARRDG----DPAPKRLASLNAAAFLKLSQERELPL-RP 223
Cdd:PHA03247  2752 GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpspwDPADPPAAVLAPAAALPPAASPAGPLpPP 2831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  224 SRAQAEADGRSTEPLAPRILRPKVNGKNCPKARQGAgSGEATGPPNWQEQPNERWPSAPPHGPPTQPSHQAPgkalENPL 303
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP-SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPE 2906
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398740  304 RPNLPllmggQAALKPEPGRPGEESPAPKQELHQPSFPAPQLSPLPMPGNPADYSGPCGGPELTAL 369
Cdd:PHA03247  2907 RPPQP-----QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
279-563 5.11e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  279 PSAPPHGPPTQPSHQAPGKALENPLRPNLPLLMGGQAALKPEPGRPGEESPAPKQELHQPSFPAP--------QLSPLPM 350
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPspapdlseMLRPVGS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  351 PGNPADYSGPCGGPELTALGSFYLYCGQDGLqcgaysPCPMLPEGKLSPVAAPNE-GLLMAPSSVPSGVPFQHPPWSAPR 429
Cdd:PHA03307   144 PGPPPAASPPAAGASPAAVASDAASSRQAAL------PLSSPEETARAPSSPPAEpPPSTPPAAASPRPPRRSSPISASA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  430 YCSSEDTGANGYSICGVLPLSLTHI--------GTTCGGCPYKMPFTAEGCR---SLGQLEFPLPEAGHPASPAHPLLGC 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSessgcgwgPENECPLPRPAPITLPTRIweaSGWNGPSSRPGPASSSSSPRERSPS 297
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398740  499 PVPSVP--PAAEPIPHLQTPISEPQTVARACPQSAKPPSGSKSGLRTGSSCRHAV--RSKAARRPSHPK 563
Cdd:PHA03307   298 PSPSSPgsGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpsRPPPPADPSSPR 366
Pacs-1 pfam10254
PACS-1 cytosolic sorting protein; PACS-1 is a cytosolic sorting protein that directs the ...
279-361 5.16e-03

PACS-1 cytosolic sorting protein; PACS-1 is a cytosolic sorting protein that directs the localization of membrane proteins in the trans-Golgi network (TGN)/endosomal system. PACS-1 connects the clathrin adaptor AP-1 to acidic cluster sorting motifs contained in the cytoplasmic domain of cargo proteins such as furin, the cation-independent mannose-6-phosphate receptor and in viral proteins such as human immunodeficiency virus type 1 Nef.


Pssm-ID: 463027  Cd Length: 416  Bit Score: 40.04  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 279 PSAPPHG----------PPTQPSHQAPGKALENPLRPNLPLLMGGQ-----AALKPEPGRPGE--ESPAPKQELhQPSFP 341
Cdd:pfam10254 234 SSSPPSSsspigkesttPPSSPSVSSGLWGPSSPSSGHGAELMELQvdywtAAQPTERKREGEkkDLPTGKNTL-KCTFR 312
                          90       100
                  ....*....|....*....|
gi 1720398740 342 APQLSPLPMPGNPADYSGPC 361
Cdd:pfam10254 313 SLQVSRLPSSGEAGATPTMS 332
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
615-725 2.93e-52

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: 177.21  E-value: 2.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPRKtSTPYVAKISALWENPEsGELMMSLLWYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVA 694
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRP-SLPYVARIESLWEDPE-GNMVVRVKWYYRPEETKGGRKPNHGE---KELFASDHQDENSVQ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720398740 695 CIEEKCYVLTFAEY---------------CRFCAMAKRRGEGLPSR 725
Cdd:cd04714    76 TIEHKCYVLTFAEYerlarvkkkpqdgvdFYYCAGTYNPDTGMLKC 121
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
615-721 3.74e-18

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: 80.90  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPRKTS-TPYVAKISALWENPEsGELMMSLLWYYRPEHLQGGRSPSMhepLQNEVFASRHQDQNSV 693
Cdd:cd04370     1 GITYEVGDSVYVEPDDSIKSdPPYIARIEELWEDTN-GSKQVKVRWFYRPEETPKGLSPFA---LRRELFLSDHLDEIPV 76
                          90       100
                  ....*....|....*....|....*...
gi 1720398740 694 ACIEEKCYVLTFAEYCRFCAMAKRRGEG 721
Cdd:cd04370    77 ESIIGKCKVLFVSEFEGLKQRPNKIDTD 104
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
616-732 2.19e-16

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: 75.81  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 616 ETIRVRDTVLLKSGPrKTSTPYVAKISALWENPESGELMMSLLWYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVAC 695
Cdd:pfam01426   1 ETYSVGDFVLVEPDD-ADEPYYVARIEELFEDTKNGKKMVRVQWFYRPEETVHRAGKAFNK---DELFLSDEEDDVPLSA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720398740 696 IEEKCYVLTFAEYCRFCAMAKRRGEGL-------PSRKTALVPP 732
Cdd:pfam01426  77 IIGKCSVLHKSDLESLDPYKIKEPDDFfcellydPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
617-720 1.37e-15

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 73.48  E-value: 1.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  617 TIRVRDTVLLKSgPRKTSTPYVAKISALWENPESGELMMSLL-WYYRPEHLQGGRSPSMHEplqNEVFASRHQDQNSVAC 695
Cdd:smart00439   1 TISVGDFVLVEP-DDADEPYYIGRIEEIFETKKNSESKMVRVrWFYRPEETVLEKAALFDK---NEVFLSDEYDTVPLSD 76
                           90       100
                   ....*....|....*....|....*
gi 1720398740  696 IEEKCYVLTFAEYCRFCAMAKRRGE 720
Cdd:smart00439  77 IIGKCNVLYKSDYPGLRPEGSIGEP 101
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
615-710 1.50e-13

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: 67.61  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSgPRKTSTPYVAKISALWENPEsGELMMSLLWYYRPEHlqggrspSMHEP----LQNEVFASRHQDQ 690
Cdd:cd04717     1 GLQYRVGDCVYVAN-PEDPSKPIIFRIERLWKDED-GEKFFFGCWFYRPEE-------TFHEPtrkfYKNEVFKSPLYET 71
                          90       100
                  ....*....|....*....|
gi 1720398740 691 NSVACIEEKCYVLTFAEYCR 710
Cdd:cd04717    72 VPVEEIVGKCAVMDVKDYIK 91
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
605-761 9.03e-13

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: 66.33  E-value: 9.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 605 RKSYQAVERHGETIRVRDTVLLKsgPRKTSTPYVAKISALWENpESGELMMSLLWYYRPEHLQGGRSPSMHEPLQNEVFA 684
Cdd:cd04713     8 KCHYTSFEKDGNKYRLEDCVLLV--PEDDQKPYIAIIKDIYKQ-EEGSLKLEVQWLYRPEEIEKKKGGNWKAEDPRELFY 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720398740 685 SRHQDQNSVACIEEKCYVlTFAeycrfcamakRRGEGLPSRKTAlvpPSadystpphrtvpedtdpelvFLCRHVYD 761
Cdd:cd04713    85 SFHRDEVPAESVLHPCKV-AFV----------PKGKQIPLRKGH---SG--------------------FIVRRVYD 127
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
606-710 4.79e-08

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


Pssm-ID: 240066  Cd Length: 159  Bit Score: 52.89  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 606 KSYQAVERHGETIRVRDTVLLKSGprkTSTPYVAKISALWENP-ESGELMMSLLWYYRPEHLQGGRSPsMHEPLQNEVFA 684
Cdd:cd04715    18 QFYRSFTYDGVEYRLYDDVYVHNG---DSEPYIGKIIKIYETAiDSGKKKVKVIWFFRPSEIRMELKG-EPKRHINEVFL 93
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720398740 685 SRHQDQ-----NSVACIEEKCYVLTFAEYCR 710
Cdd:cd04715    94 ACGRGEglaniNLLESIIGKCNVVCISEDFR 124
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
613-716 4.58e-05

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


Pssm-ID: 240072  Cd Length: 130  Bit Score: 43.59  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 613 RHGETIRVRDTVLLKSGPRKTstpYVAKISALWENpESGELMMSLLWYYRPEHLQGGRSPSMHEPlqNEVFASRHQDQNS 692
Cdd:cd04721     3 RNGVTISVHDFVYVLSEEEDR---YVAYIEDLYED-KKGSKMVKVRWFHTTDEVGAALSPDSVNP--REIFLSPNLQVIS 76
                          90       100
                  ....*....|....*....|....
gi 1720398740 693 VACIEEKCYVLTFAEYCRFCAMAK 716
Cdd:cd04721    77 VECIDGLATVLTREHYEKFQSVPK 100
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
615-703 2.13e-04

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


Pssm-ID: 240067  Cd Length: 122  Bit Score: 41.66  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPRKTstPYVAKISALWENPEsGELMMSLLWYYRPEHLQGGRSPSMHEPlqNEVFASRHQDQNSVA 694
Cdd:cd04716     1 GITYNLGDDAYVQGGEGEE--PFICKITEFFEGTD-GKTYFTAQWFYRAEDTVIERQATNHDK--KRVFYSEIKNDNPLD 75

                  ....*....
gi 1720398740 695 CIEEKCYVL 703
Cdd:cd04716    76 CLISKVKIL 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
149-369 2.20e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  149 GDPHRSRDRATGSWSFSKKRPRLGDLGEGSRDLSPELAPDEGARRDG----DPAPKRLASLNAAAFLKLSQERELPL-RP 223
Cdd:PHA03247  2752 GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpspwDPADPPAAVLAPAAALPPAASPAGPLpPP 2831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  224 SRAQAEADGRSTEPLAPRILRPKVNGKNCPKARQGAgSGEATGPPNWQEQPNERWPSAPPHGPPTQPSHQAPgkalENPL 303
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP-SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPE 2906
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398740  304 RPNLPllmggQAALKPEPGRPGEESPAPKQELHQPSFPAPQLSPLPMPGNPADYSGPCGGPELTAL 369
Cdd:PHA03247  2907 RPPQP-----QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
619-707 7.18e-04

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: 40.84  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 619 RVRDTVLLKSGPrktSTPYV-AKISALWENPeSGELMMSLLWYYR----PEHL-------------QGGRSPSM--HEPL 678
Cdd:cd04709     5 RVGDYVYFESSP---NNPYLiRRIEELNKTA-RGHVEAKVVCYYRrrdiPDSLyqladqhrreleeKSDDLTPKqrHQLR 80
                          90       100
                  ....*....|....*....|....*....
gi 1720398740 679 QNEVFASRHQDQNSVACIEEKCYVLTFAE 707
Cdd:cd04709    81 HRELFLSRQVETLPATHIRGKCSVTLLND 109
BAH_Orc1p_Yeast cd04720
BAH, or Bromo Adjacent Homology domain, as present in Orc1p, which again is part of the ...
615-761 1.76e-03

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


Pssm-ID: 240071  Cd Length: 179  Bit Score: 40.09  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 615 GETIRVRDTVLLKSGPrkTSTPYVAKISALWENPESGELMMSLLWYYRPEHLQGGRSPSMHEPL------QNEVFASRHQ 688
Cdd:cd04720    50 GLELSVGDTILVKDDV--ANSPSVYLIHEIRLNTLNNEVELWVMWFLRWFEINPARYYKQFDPEfrsesnKNELYLTAEL 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720398740 689 DQNSVACIEEKCYVLTFAEYcrfcamakrrgeglpsrktalvppsadystppHRTVPEDTDPELVFLCRHVYD 761
Cdd:cd04720   128 SEIKLKDIIDKANVLSESEF--------------------------------NDLSTDDKNGERTFFCRYACE 168
PHA03247 PHA03247
large tegument protein UL36; Provisional
197-540 1.78e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  197 PAPKRLASLNAAAFLKLSQERELPLRPSRAQAEADGRSTEPLAPRILRPKvngkncpKARQGAGSGEATGPPNWQEQPNE 276
Cdd:PHA03247  2616 PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR-------RARRLGRAAQASSPPQRPRRRAA 2688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  277 RWPSAP------PHGPPTQPSHQAPgkalenPLRPNLPLLMGGQAALKPEPGRPGEES-PAPKQELHQPSFPAPQLSP-- 347
Cdd:PHA03247  2689 RPTVGSltsladPPPPPPTPEPAPH------ALVSATPLPPGPAAARQASPALPAAPApPAVPAGPATPGGPARPARPpt 2762
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  348 LPMPGNPADYSGPCGGPELTALGSfylyCGQDGLQCGAYSPCPMLPEGKLSPVAAPNEGLLM----APSSVPSGVPFQHP 423
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPPRRLTRP----AVASLSESRESLPSPWDPADPPAAVLAPAAALPPaaspAGPLPPPTSAQPTA 2838
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  424 PWSAPRYCSSEDTGANGYSICGvlplSLTHIGTTCGGCPYKMPFTAEGCRSLGQLEFPLPEAGHPASPAHPLLGCPVPSV 503
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGG----DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1720398740  504 PPAAEPIPHLQTPISEPQTVARACPQSAKPPSGSKSG 540
Cdd:PHA03247  2915 PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
613-702 2.03e-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: 39.28  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 613 RHGETIRVRDTVLLKSGPrkTSTPY-VAKISALWENPE-----------SGELMMSLLWYYRPEHLQggRSPSMHEPLqn 680
Cdd:cd04710     7 KNGELLKVNDHIYMSSEP--PGEPYyIGRIMEFVPKHEfpsgiharvfpASYFQVRLNWYYRPRDIS--RRVVADSRL-- 80
                          90       100
                  ....*....|....*....|..
gi 1720398740 681 eVFASRHQDQNSVACIEEKCYV 702
Cdd:cd04710    81 -LYASMHSDICPIGSVRGKCTV 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
223-355 2.70e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  223 PSRAQAEADGRSTEPLAPRILRPKVNGKNCPKARqgagsgeatgPPNWQEQPNERWPSAPPHGPPTQPSHQAPGKALENP 302
Cdd:PHA03247  2867 PSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL----------PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720398740  303 LRPNLPL--LMGGQAALKPEPGRPGE--------ESPAPKQELHQ--PSFPAPQLSPLPMPGNPA 355
Cdd:PHA03247  2937 PRPQPPLapTTDPAGAGEPSGAVPQPwlgalvpgRVAVPRFRVPQpaPSREAPASSTPPLTGHSL 3001
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
279-563 5.11e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  279 PSAPPHGPPTQPSHQAPGKALENPLRPNLPLLMGGQAALKPEPGRPGEESPAPKQELHQPSFPAP--------QLSPLPM 350
Cdd:PHA03307    64 RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPspapdlseMLRPVGS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  351 PGNPADYSGPCGGPELTALGSFYLYCGQDGLqcgaysPCPMLPEGKLSPVAAPNE-GLLMAPSSVPSGVPFQHPPWSAPR 429
Cdd:PHA03307   144 PGPPPAASPPAAGASPAAVASDAASSRQAAL------PLSSPEETARAPSSPPAEpPPSTPPAAASPRPPRRSSPISASA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740  430 YCSSEDTGANGYSICGVLPLSLTHI--------GTTCGGCPYKMPFTAEGCR---SLGQLEFPLPEAGHPASPAHPLLGC 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSessgcgwgPENECPLPRPAPITLPTRIweaSGWNGPSSRPGPASSSSSPRERSPS 297
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398740  499 PVPSVP--PAAEPIPHLQTPISEPQTVARACPQSAKPPSGSKSGLRTGSSCRHAV--RSKAARRPSHPK 563
Cdd:PHA03307   298 PSPSSPgsGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSpsRPPPPADPSSPR 366
Pacs-1 pfam10254
PACS-1 cytosolic sorting protein; PACS-1 is a cytosolic sorting protein that directs the ...
279-361 5.16e-03

PACS-1 cytosolic sorting protein; PACS-1 is a cytosolic sorting protein that directs the localization of membrane proteins in the trans-Golgi network (TGN)/endosomal system. PACS-1 connects the clathrin adaptor AP-1 to acidic cluster sorting motifs contained in the cytoplasmic domain of cargo proteins such as furin, the cation-independent mannose-6-phosphate receptor and in viral proteins such as human immunodeficiency virus type 1 Nef.


Pssm-ID: 463027  Cd Length: 416  Bit Score: 40.04  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398740 279 PSAPPHG----------PPTQPSHQAPGKALENPLRPNLPLLMGGQ-----AALKPEPGRPGE--ESPAPKQELhQPSFP 341
Cdd:pfam10254 234 SSSPPSSsspigkesttPPSSPSVSSGLWGPSSPSSGHGAELMELQvdywtAAQPTERKREGEkkDLPTGKNTL-KCTFR 312
                          90       100
                  ....*....|....*....|
gi 1720398740 342 APQLSPLPMPGNPADYSGPC 361
Cdd:pfam10254 313 SLQVSRLPSSGEAGATPTMS 332
 
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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