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Conserved domains on  [gi|1865418624|gb|KAF5477862|]
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hypothetical protein F2P56_004475 [Juglans regia]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAH super family cl02608
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
500-616 1.16e-45

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.


The actual alignment was detected with superfamily member cd04716:

Pssm-ID: 470629  Cd Length: 122  Bit Score: 160.30  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  500 NHIFSLGDCAYIKGDGGQ-KHIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGAFHNKRRLFYSTIMNDNLIDCIISK 578
Cdd:cd04716      1 GITYNLGDDAYVQGGEGEePFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQATNHDKKRVFYSEIKNDNPLDCLISK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1865418624  579 VSVTQITPRVG--RILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:cd04716     81 VKILQVPPNVGtkRKKPNSEKCDYYYDMEYCVPYSTFQTL 120
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
760-816 2.26e-33

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349285  Cd Length: 57  Bit Score: 122.42  E-value: 2.26e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDICYGDPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18635      1 EFEVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEFVQ 57
Dcm super family cl43082
DNA-cytosine methylase [Replication, recombination and repair];
657-988 5.42e-28

DNA-cytosine methylase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0270:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 114.91  E-value: 5.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  657 KLALLDLFSGCGGMStgmcLGAKLTGVNLAmrWALDSDGSACESLKLNHPETLVRNEtaadflellmeweklcghyrlng 736
Cdd:COG0270      3 KLTVIDLFAGAGGLS----LGFEKAGFEVV--FAVEIDPDACETYRANFPEAKVIEG----------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  737 agrthpsrvmtsgadscngiptgeyevsrlvDIcygdpnktgkRGLNFKvhwkgystsedtwepieglsncqeriqdfvq 816
Cdd:COG0270     54 -------------------------------DI----------RDIDPE------------------------------- 61
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  817 nglkskilPLPGDVDVICGGPPCQGISGYNRYRNIDsplsDDRNRQIVVFMDIVTFLKPKFVLMENVVDILRFDKASLGR 896
Cdd:COG0270     62 --------ELIPDVDLLIGGPPCQPFSVAGKRKGLE----DPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFE 129
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  897 YALSRLVHMNYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTHdvivrywpppeferntvayeedqpreLEE 976
Cdd:COG0270    130 EILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH--------------------------LKP 183
                          330
                   ....*....|..
gi 1865418624  977 ALVLRDAISDLP 988
Cdd:COG0270    184 YVTVGDALEDLP 195
 
Name Accession Description Interval E-value
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
500-616 1.16e-45

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: 160.30  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  500 NHIFSLGDCAYIKGDGGQ-KHIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGAFHNKRRLFYSTIMNDNLIDCIISK 578
Cdd:cd04716      1 GITYNLGDDAYVQGGEGEePFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQATNHDKKRVFYSEIKNDNPLDCLISK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1865418624  579 VSVTQITPRVG--RILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:cd04716     81 VKILQVPPNVGtkRKKPNSEKCDYYYDMEYCVPYSTFQTL 120
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
760-816 2.26e-33

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 122.42  E-value: 2.26e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDICYGDPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18635      1 EFEVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEFVQ 57
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
657-988 5.42e-28

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 114.91  E-value: 5.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  657 KLALLDLFSGCGGMStgmcLGAKLTGVNLAmrWALDSDGSACESLKLNHPETLVRNEtaadflellmeweklcghyrlng 736
Cdd:COG0270      3 KLTVIDLFAGAGGLS----LGFEKAGFEVV--FAVEIDPDACETYRANFPEAKVIEG----------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  737 agrthpsrvmtsgadscngiptgeyevsrlvDIcygdpnktgkRGLNFKvhwkgystsedtwepieglsncqeriqdfvq 816
Cdd:COG0270     54 -------------------------------DI----------RDIDPE------------------------------- 61
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  817 nglkskilPLPGDVDVICGGPPCQGISGYNRYRNIDsplsDDRNRQIVVFMDIVTFLKPKFVLMENVVDILRFDKASLGR 896
Cdd:COG0270     62 --------ELIPDVDLLIGGPPCQPFSVAGKRKGLE----DPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFE 129
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  897 YALSRLVHMNYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTHdvivrywpppeferntvayeedqpreLEE 976
Cdd:COG0270    130 EILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH--------------------------LKP 183
                          330
                   ....*....|..
gi 1865418624  977 ALVLRDAISDLP 988
Cdd:COG0270    184 YVTVGDALEDLP 195
BAH smart00439
Bromo adjacent homology domain;
502-616 2.52e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 93.51  E-value: 2.52e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624   502 IFSLGDCAYIKGDGGQK--HIGRILEFFRTTDGEN--YFRVQWFYKVEDTvIKEEGAFHNKRRLFYSTIMNDNLIDCIIS 577
Cdd:smart00439    1 TISVGDFVLVEPDDADEpyYIGRIEEIFETKKNSEskMVRVRWFYRPEET-VLEKAALFDKNEVFLSDEYDTVPLSDIIG 79
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1865418624   578 KVSVTQITPRVG--RILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:smart00439   80 KCNVLYKSDYPGlrPEGSIGEPDVFFCESAYDPEKGSFKKL 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
502-616 1.72e-13

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: 68.10  E-value: 1.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  502 IFSLGDCAYIKGDGGQK--HIGRILEFFRTTDGEN-YFRVQWFYKVEDTViKEEGAFHNKRRLFYSTIMNDNLIDCIISK 578
Cdd:pfam01426    2 TYSVGDFVLVEPDDADEpyYVARIEELFEDTKNGKkMVRVQWFYRPEETV-HRAGKAFNKDELFLSDEEDDVPLSAIIGK 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1865418624  579 VSVTQITP-RVGRILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:pfam01426   81 CSVLHKSDlESLDPYKIKEPDDFFCELLYDPKTKSFKKL 119
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
826-1012 1.29e-12

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or 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.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 69.57  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  826 LPGDVDVICGGPPCQGIS--GYNRYRNidsplsDDRNRQIVVFMDIVTFLKPKFVLMENVVDILRFDKaslGRYA---LS 900
Cdd:cd00315     59 FIPDIDLLTGGFPCQPFSiaGKRKGFE------DTRGTLFFEIIRILKEKKPKYFLLENVKGLLTHDN---GNTLkviLN 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  901 RLVHMNYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTH---------DVIvrYWPPPEFERNTVA--YEED 969
Cdd:cd00315    130 TLEELGYNVYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKpsekkktlkDIL--RIRDPDEPSPTLTasYGKG 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1865418624  970 QPRELEEALVLRDAISDLPAVTnfeIReEMSR--------EKPPETDFQRY 1012
Cdd:cd00315    208 TGSVHPTAPDMIGKESNIRRLT---PR-ECARlqgfpddfEFPGKSVTQAY 254
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
761-816 2.86e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 62.21  E-value: 2.86e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1865418624  761 YEVSRLVDICYGDpnktgKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:pfam00385    1 YEVERILDHRKDK-----GGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
760-816 1.28e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 60.69  E-value: 1.28e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624   760 EYEVSRLVDICYgdpnkTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:smart00298    1 EYEVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKK 52
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
829-948 5.58e-11

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 65.04  E-value: 5.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  829 DVDVICGGPPCQGISgYNRYRNidsPLSDDRNrqiVVFMDIVTFLK---PKFVLMENVVDILRFDKASLGRYALSRLVHM 905
Cdd:TIGR00675   59 DFDILLGGFPCQPFS-IAGKRK---GFEDTRG---TLFFEIVRILKekkPKFFLLENVKGLVSHDKGRTFKVIIETLEEL 131
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1865418624  906 NYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTHD 948
Cdd:TIGR00675  132 GYKVYYKVLNAKDFGVPQNRERIYIVGFRDFDDKLNFEFPKPI 174
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
829-1018 2.09e-10

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 63.49  E-value: 2.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  829 DVDVICGGPPCQGIS--GYNRyrnidsPLSDDRNrqiVVFMDIVTFLK---PKFVLMENVVDILRFDKASLGRYALSRLV 903
Cdd:pfam00145   60 DIDILTGGFPCQDFSiaGKQK------GFEDTRG---TLFFEIIRIIKekkPKAFLLENVKGLLSHDNGNTLNVILETLE 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  904 HMNYQARLGTIAAGCYGLPQFRLRVFLWGAH------PSEKLPQF----PLPTHDVIVRYWPPPEFERNTVAYE----ED 969
Cdd:pfam00145  131 ELGYHVSWKVLNASDYGVPQNRERVFIVGIRkdlnlnVLVPVPEFdfpkPKDLTGTIRDLLEEPSLDENKYNLSdkfvEN 210
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1865418624  970 QPRELEEALVLRDAISDlpavtnfeireEMSREKPPETDFQRYIRSTRY 1018
Cdd:pfam00145  211 HERRKPTTKAPGGGYPT-----------YLLRNRIDKVEEGKGPSFTYR 248
 
Name Accession Description Interval E-value
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
500-616 1.16e-45

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: 160.30  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  500 NHIFSLGDCAYIKGDGGQ-KHIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGAFHNKRRLFYSTIMNDNLIDCIISK 578
Cdd:cd04716      1 GITYNLGDDAYVQGGEGEePFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQATNHDKKRVFYSEIKNDNPLDCLISK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1865418624  579 VSVTQITPRVG--RILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:cd04716     81 VKILQVPPNVGtkRKKPNSEKCDYYYDMEYCVPYSTFQTL 120
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
760-816 2.26e-33

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 122.42  E-value: 2.26e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDICYGDPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18635      1 EFEVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEFVQ 57
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
657-988 5.42e-28

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 114.91  E-value: 5.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  657 KLALLDLFSGCGGMStgmcLGAKLTGVNLAmrWALDSDGSACESLKLNHPETLVRNEtaadflellmeweklcghyrlng 736
Cdd:COG0270      3 KLTVIDLFAGAGGLS----LGFEKAGFEVV--FAVEIDPDACETYRANFPEAKVIEG----------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  737 agrthpsrvmtsgadscngiptgeyevsrlvDIcygdpnktgkRGLNFKvhwkgystsedtwepieglsncqeriqdfvq 816
Cdd:COG0270     54 -------------------------------DI----------RDIDPE------------------------------- 61
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  817 nglkskilPLPGDVDVICGGPPCQGISGYNRYRNIDsplsDDRNRQIVVFMDIVTFLKPKFVLMENVVDILRFDKASLGR 896
Cdd:COG0270     62 --------ELIPDVDLLIGGPPCQPFSVAGKRKGLE----DPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFE 129
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  897 YALSRLVHMNYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTHdvivrywpppeferntvayeedqpreLEE 976
Cdd:COG0270    130 EILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH--------------------------LKP 183
                          330
                   ....*....|..
gi 1865418624  977 ALVLRDAISDLP 988
Cdd:COG0270    184 YVTVGDALEDLP 195
BAH smart00439
Bromo adjacent homology domain;
502-616 2.52e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 93.51  E-value: 2.52e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624   502 IFSLGDCAYIKGDGGQK--HIGRILEFFRTTDGEN--YFRVQWFYKVEDTvIKEEGAFHNKRRLFYSTIMNDNLIDCIIS 577
Cdd:smart00439    1 TISVGDFVLVEPDDADEpyYIGRIEEIFETKKNSEskMVRVRWFYRPEET-VLEKAALFDKNEVFLSDEYDTVPLSDIIG 79
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1865418624   578 KVSVTQITPRVG--RILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:smart00439   80 KCNVLYKSDYPGlrPEGSIGEPDVFFCESAYDPEKGSFKKL 120
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
502-616 9.02e-21

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: 88.99  E-value: 9.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  502 IFSLGDCAYIKGDGGQK----HIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGaFHNKRRLFYSTIMNDNLIDCIIS 577
Cdd:cd04370      3 TYEVGDSVYVEPDDSIKsdppYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSP-FALRRELFLSDHLDEIPVESIIG 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1865418624  578 KVSVTQITP--RVGRILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:cd04370     82 KCKVLFVSEfeGLKQRPNKIDTDDFFCRLAYDPTTKEFKAL 122
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
502-616 1.72e-13

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: 68.10  E-value: 1.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  502 IFSLGDCAYIKGDGGQK--HIGRILEFFRTTDGEN-YFRVQWFYKVEDTViKEEGAFHNKRRLFYSTIMNDNLIDCIISK 578
Cdd:pfam01426    2 TYSVGDFVLVEPDDADEpyYVARIEELFEDTKNGKkMVRVQWFYRPEETV-HRAGKAFNKDELFLSDEEDDVPLSAIIGK 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1865418624  579 VSVTQITP-RVGRILNFILPSDFYFDMEYCVDYSTFRSL 616
Cdd:pfam01426   81 CSVLHKSDlESLDPYKIKEPDDFFCELLYDPKTKSFKKL 119
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
826-1012 1.29e-12

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or 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.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 69.57  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  826 LPGDVDVICGGPPCQGIS--GYNRYRNidsplsDDRNRQIVVFMDIVTFLKPKFVLMENVVDILRFDKaslGRYA---LS 900
Cdd:cd00315     59 FIPDIDLLTGGFPCQPFSiaGKRKGFE------DTRGTLFFEIIRILKEKKPKYFLLENVKGLLTHDN---GNTLkviLN 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  901 RLVHMNYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTH---------DVIvrYWPPPEFERNTVA--YEED 969
Cdd:cd00315    130 TLEELGYNVYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKpsekkktlkDIL--RIRDPDEPSPTLTasYGKG 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1865418624  970 QPRELEEALVLRDAISDLPAVTnfeIReEMSR--------EKPPETDFQRY 1012
Cdd:cd00315    208 TGSVHPTAPDMIGKESNIRRLT---PR-ECARlqgfpddfEFPGKSVTQAY 254
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
761-816 2.86e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 62.21  E-value: 2.86e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1865418624  761 YEVSRLVDICYGDpnktgKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:pfam00385    1 YEVERILDHRKDK-----GGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKD 51
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
761-814 1.12e-11

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 60.57  E-value: 1.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1865418624  761 YEVSRLVDIcygdpnKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd00024      1 YEVEKILDH------RVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEY 48
CHROMO smart00298
Chromatin organization modifier domain;
760-816 1.28e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 60.69  E-value: 1.28e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624   760 EYEVSRLVDICYgdpnkTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:smart00298    1 EYEVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKK 52
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
829-948 5.58e-11

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 65.04  E-value: 5.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  829 DVDVICGGPPCQGISgYNRYRNidsPLSDDRNrqiVVFMDIVTFLK---PKFVLMENVVDILRFDKASLGRYALSRLVHM 905
Cdd:TIGR00675   59 DFDILLGGFPCQPFS-IAGKRK---GFEDTRG---TLFFEIVRILKekkPKFFLLENVKGLVSHDKGRTFKVIIETLEEL 131
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1865418624  906 NYQARLGTIAAGCYGLPQFRLRVFLWGAHPSEKLPQFPLPTHD 948
Cdd:TIGR00675  132 GYKVYYKVLNAKDFGVPQNRERIYIVGFRDFDDKLNFEFPKPI 174
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
829-1018 2.09e-10

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 63.49  E-value: 2.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  829 DVDVICGGPPCQGIS--GYNRyrnidsPLSDDRNrqiVVFMDIVTFLK---PKFVLMENVVDILRFDKASLGRYALSRLV 903
Cdd:pfam00145   60 DIDILTGGFPCQDFSiaGKQK------GFEDTRG---TLFFEIIRIIKekkPKAFLLENVKGLLSHDNGNTLNVILETLE 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  904 HMNYQARLGTIAAGCYGLPQFRLRVFLWGAH------PSEKLPQF----PLPTHDVIVRYWPPPEFERNTVAYE----ED 969
Cdd:pfam00145  131 ELGYHVSWKVLNASDYGVPQNRERVFIVGIRkdlnlnVLVPVPEFdfpkPKDLTGTIRDLLEEPSLDENKYNLSdkfvEN 210
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1865418624  970 QPRELEEALVLRDAISDlpavtnfeireEMSREKPPETDFQRYIRSTRY 1018
Cdd:pfam00145  211 HERRKPTTKAPGGGYPT-----------YLLRNRIDKVEEGKGPSFTYR 248
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
502-581 2.50e-10

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: 59.14  E-value: 2.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  502 IFSLGDCAYIK--GDGGQKHIGRILEFFRTTDGENYFRVQWFYKVEDTvikeegaFHNKRRLFY------STIMNDNLID 573
Cdd:cd04717      3 QYRVGDCVYVAnpEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEET-------FHEPTRKFYknevfkSPLYETVPVE 75

                   ....*...
gi 1865418624  574 CIISKVSV 581
Cdd:cd04717     76 EIVGKCAV 83
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
760-814 9.22e-09

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


Pssm-ID: 349284  Cd Length: 52  Bit Score: 52.45  E-value: 9.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDicyGDPNKTGKrgLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18634      1 LYEVERIVD---KRKNKKGK--TEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDF 50
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
760-814 9.70e-09

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 52.35  E-value: 9.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDICYGDPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18968      1 EYEVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
760-818 5.10e-08

N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of cryptic loci regulator 4 (Clr4), a histone H3 lysine methyltransferase which targets H3K9. Clr4 regulates silencing and switching at the mating-type loci and affects chromatin structure at centromeres. Clr4 is a catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349282  Cd Length: 55  Bit Score: 50.58  E-value: 5.10e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1865418624  760 EYEVSRLVDicygDPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQNG 818
Cdd:cd18632      1 EYEVEKIVD----EKTDRNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRKK 55
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
760-814 7.18e-08

chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Trichosporon asahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349336  Cd Length: 56  Bit Score: 50.26  E-value: 7.18e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDICYGDPNKTGKRGLnfkVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18980      3 EYEVEAILDHKVDRRYRDPNFYL---VRWRGYGPSHDSWEPTSALENAQDLLREF 54
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
761-814 1.26e-07

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349283  Cd Length: 51  Bit Score: 49.21  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1865418624  761 YEVSRLVDIcygdpnKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18633      2 FEVEKILDM------KTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEF 49
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
760-814 1.23e-06

chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a.


Pssm-ID: 349300  Cd Length: 50  Bit Score: 46.56  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLsNCQERIQDF 814
Cdd:cd18653      1 EYAVEKICD------RRVRKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
761-816 5.25e-06

chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain


Pssm-ID: 349328  Cd Length: 50  Bit Score: 44.43  E-value: 5.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18972      1 YEVEAIVG------HKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK 50
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
760-816 3.00e-05

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349281  Cd Length: 50  Bit Score: 42.42  E-value: 3.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865418624  760 EYEVSRLVDicygdpnktgKRGLNFKVH----WKGYSTSEDTWEPIEGLsNCQERIQDFVQ 816
Cdd:cd18631      1 EYVVEKVLD----------RRVVKGKVEyllkWKGYPDEDNTWEPEENL-DCPDLIAEFEE 50
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
760-814 5.99e-05

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members of this subgroup, the chromodomain is followed by a chromo shadow domain; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. For the majority of members of this subgroup, the chromodomain is followed by a chromo shadow domain (CSD).


Pssm-ID: 349325  Cd Length: 56  Bit Score: 41.74  E-value: 5.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDICYGdpnKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18969      3 EYEIEEILDVKKG---GFEDGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEY 54
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
761-814 6.12e-05

chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This subgroup includes the N-terminal CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 (HP1)-like protein from Entamoeba histolytica, and similar proteins. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349288  Cd Length: 52  Bit Score: 41.86  E-value: 6.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGL-SNCQERIQDF 814
Cdd:cd18638      2 FEVEKIVK------KKTVKGGTEYFVKWKGYSAKENTWETEDNLeKSYKEMIDEF 50
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
778-814 6.57e-05

chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of Drosophila melanogaster Rhino (also known as heterochromatin protein 1-like), and similar proteins. Rhino is a female-specific protein that affects chromosome structure and egg polarity that is required for germline PIWI-interacting RNA (piRNA) production. In Drosophila the RDC (rhino, deadlock, and cutoff) complex, composed of rhino, the protein deadlock (Del) and the Rai1-like transcription termination cofactor cutoff (Cuff) binds to chromatin of dual-strand piRNA clusters, special genomic regions, which encode piRNA precursors. The RDC complex is anchored to H3K9me3-marked chromatin in part via the H3K9me3-binding activity of Rhino, and is required for transcription of piRNA precursors. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349280  Cd Length: 51  Bit Score: 41.74  E-value: 6.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1865418624  778 GKRGLN----FKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18630      9 GKRFVNgrpqVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
779-814 1.25e-04

chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349290  Cd Length: 52  Bit Score: 40.74  E-value: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1865418624  779 KRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18640     15 KKTWEYLVKWENRSHHENTWEPMANLERCKYLLQMF 50
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
761-816 1.66e-04

chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349329  Cd Length: 50  Bit Score: 40.31  E-value: 1.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18973      1 YVVEAILD------NKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ 50
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
491-564 1.85e-04

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: 42.84  E-value: 1.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  491 SHYAQAKLNNHIFSLGDCAYIKGDGGQK-HIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGAF--HNKRRLFYS 564
Cdd:cd04713      9 CHYTSFEKDGNKYRLEDCVLLVPEDDQKpYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKKGGNWkaEDPRELFYS 85
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
511-616 1.91e-04

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: 42.39  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  511 IKGDGGQKHIGRILEFFRTTDGENYFRVQWFYKVEDTVIkeeGAFHNKRRLFYS----TIMNDNLIDCIISKVSVT-QIT 585
Cdd:cd04712     26 NDDHRWLPLVQFVEYMKKGSDGSKMFHGRWLYRGCDTVL---GNYANERELFLTnectCLELDLLSTEIKGVHKVDwSGT 102
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1865418624  586 PRVGrilnfILPSDFYFDMEYCVDYSTFRSL 616
Cdd:cd04712    103 PWGK-----GLPEFFVRQSYYWPERGAFTSL 128
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
502-581 4.15e-04

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: 41.23  E-value: 4.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  502 IFSLGDCAYIK--GDGGQKHIGRILEFFRTTDGENYFRVQWFYKVEDTvikeEGA---FHNKRRLFYSTIMNDNLIDCII 576
Cdd:cd04714      3 IIRVGDCVLFKspGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEET----KGGrkpNHGEKELFASDHQDENSVQTIE 78

                   ....*
gi 1865418624  577 SKVSV 581
Cdd:cd04714     79 HKCYV 83
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
760-816 4.29e-04

chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349334  Cd Length: 52  Bit Score: 39.22  E-value: 4.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLsNCQERIQDFVQ 816
Cdd:cd18978      3 SYEVEKIIN------HRGEKNRRKYLVKWKGYDDTDNSWVTQEDF-NDKDMIDEYEN 52
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
779-816 4.42e-04

chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog gamma (also known as HP1gamma, Cbx3, and Chromobox 3), and related proteins. HP1gamma is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. In addition to being involved in transcriptional silencing in heterochromatin-like complexes, HP1gamma also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma.


Pssm-ID: 349299  Cd Length: 50  Bit Score: 39.22  E-value: 4.42e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1865418624  779 KRGLNFKVH----WKGYSTSEDTWEPIEGLsNCQERIQDFVQ 816
Cdd:cd18652     10 RRVVNGKVEyflkWKGFTDADNTWEPEENL-DCPELIEAFLN 50
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
760-816 6.45e-04

chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3).


Pssm-ID: 349297  Cd Length: 50  Bit Score: 38.77  E-value: 6.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLsNCQERIQDFVQ 816
Cdd:cd18650      1 EYVVEKVLD------RRVVKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEFLQ 50
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
761-814 8.92e-04

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349289  Cd Length: 49  Bit Score: 38.27  E-value: 8.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLsNCQERIQDF 814
Cdd:cd18639      1 YEVEYLCD------YKKIREQEYYLVKWKGYPDSENTWEPRQNL-KCSRLLKQF 47
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
760-816 1.46e-03

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 37.66  E-value: 1.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865418624  760 EYEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLsNCQERIQDFVQ 816
Cdd:cd18651      1 EYVVEKVLD------RRVVKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEFMK 50
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
761-814 2.22e-03

chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in uncharacterized putative retrotransposon proteins, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349332  Cd Length: 51  Bit Score: 37.16  E-value: 2.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSN-CQERIQDF 814
Cdd:cd18976      1 YIVESLLD------RRKVRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAY 49
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
760-814 2.63e-03

chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Rhizoctonia solani AG-3 Rhs1AP, a putative Ty3/Gypsy polyprotein/retrotransposon which includes a protease, a reverse transcriptase, a ribonuclease H, and an integrase domain, in that order, with a chromodomain at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349333  Cd Length: 57  Bit Score: 37.08  E-value: 2.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  760 EYEVSRLVDICYgdPNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18977      3 EYEVEKIVGEKW--KKRKNRRVKLYKVRFKGYGPEEDEWLTKEELKNAPEILAEW 55
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
777-804 3.13e-03

chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349335  Cd Length: 48  Bit Score: 36.70  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|....*...
gi 1865418624  777 TGKRGLNFKVHWKGYSTSEDTWEPIEGL 804
Cdd:cd18979     12 RDKGNKEFLVQWQGLSVEEATWEPYKDL 39
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
761-814 3.65e-03

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 36.69  E-value: 3.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18974      1 WEVEEIVD------EKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSY 48
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
761-814 5.32e-03

chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349286  Cd Length: 52  Bit Score: 36.27  E-value: 5.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1865418624  761 YEVSRlvdICYGDPNKTGKRglNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDF 814
Cdd:cd18636      2 YEVED---ILADRVNKNGIN--EYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKW 50
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
506-586 6.96e-03

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. 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: 240107  Cd Length: 124  Bit Score: 37.83  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  506 GDCAYIKGD--GGQKHIGRILEFFRTTDGENYFRVQWFYKVEDTVIKEEGafhNKRRLFYSTIMNDNLIDCIISKVSVTQ 583
Cdd:cd04760      7 GDCVSVKPDdpTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETS---DPLELFLVDECEDMALSSIHGKVNVIY 83

                   ...
gi 1865418624  584 ITP 586
Cdd:cd04760     84 KAP 86
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
761-814 7.07e-03

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 36.00  E-value: 7.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1865418624  761 YEVSRLVDicygdpNKTGKRGLN-FKVHWKGYSTSEDTWEPIEGLsNCQERIQDF 814
Cdd:cd18960      2 FVVERILD------KRLGRNGGEeFLIKWQGFPESDSSWEPRENL-QCDEMLEEF 49
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
493-585 8.29e-03

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: 38.25  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865418624  493 YAQAKLNNHIFSLGDCAYIKGDGGQKHIGRILEFFRTT--DGENYFRVQWFYKVEDtvIKEEGAFHNKR---RLFYST-- 565
Cdd:cd04715     20 YRSFTYDGVEYRLYDDVYVHNGDSEPYIGKIIKIYETAidSGKKKVKVIWFFRPSE--IRMELKGEPKRhinEVFLACgr 97
                           90       100
                   ....*....|....*....|...
gi 1865418624  566 ---IMNDNLIDCIISKVSVTQIT 585
Cdd:cd04715     98 gegLANINLLESIIGKCNVVCIS 120
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
776-816 8.41e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 35.77  E-value: 8.41e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1865418624  776 KTGKRGLNFKVHWKGYSTSEDTWEPIEGLSNCQERIQDFVQ 816
Cdd:cd18964     14 RDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK 54
 
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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