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Conserved domains on  [gi|225543402|ref|NP_076262|]
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M-phase phosphoprotein 8 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
541-722 1.87e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 541 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 620
Cdd:COG0666   64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 621 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 700
Cdd:COG0666  142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                        170       180
                 ....*....|....*....|..
gi 225543402 701 ALYFAKQCNNVLVYELLKSHLE 722
Cdd:COG0666  222 ALDLAAENGNLEIVKLLLEAGA 243
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 7.92e-31

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: 114.69  E-value: 7.92e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225543402  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633    1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PTZ00121 super family cl31754
MAEBL; Provisional
 97-470 3.20e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121 1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTL--------KSSRLSGEEKSLKSPDLA 404
Cdd:PTZ00121 1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeakiKAEELKKAEEEKKKVEQL 1638

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402  405 EEEKEKKNEPKGKYQK---RYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 470
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
541-722 1.87e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 541 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 620
Cdd:COG0666   64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 621 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 700
Cdd:COG0666  142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                        170       180
                 ....*....|....*....|..
gi 225543402 701 ALYFAKQCNNVLVYELLKSHLE 722
Cdd:COG0666  222 ALDLAAENGNLEIVKLLLEAGA 243
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 7.92e-31

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: 114.69  E-value: 7.92e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225543402  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633    1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-693 4.67e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  604 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 683
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 225543402  684 VIECGADCNI 693
Cdd:pfam12796  80 LLEKGADINV 89
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 1.53e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 65.68  E-value: 1.53e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 225543402   59 FEVERILDMK-CEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRkDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
58-109 3.56e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 61.85  E-value: 3.56e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 225543402    58 VFEVERILDMKCEGGKNL-YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 617-719 1.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 617 LLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSK 696
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                         90       100
                 ....*....|....*....|....
gi 225543402 697 HqnsALYFA-KQCNNVLVYELLKS 719
Cdd:PHA03100 257 T---LLYFKdKDLNTITKIKMLKK 277
PTZ00121 PTZ00121
MAEBL; Provisional
 97-470 3.20e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121 1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTL--------KSSRLSGEEKSLKSPDLA 404
Cdd:PTZ00121 1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeakiKAEELKKAEEEKKKVEQL 1638

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402  405 EEEKEKKNEPKGKYQK---RYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 470
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 664-693 5.90e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 5.90e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 225543402   664 NGETALMKACKRGNSDIVRLVIECGADCNI 693
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 560-722 9.28e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  560 TNRIPNNLLRDAVKNGDYIAVKVALnsneeYNLDQEDSTGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQK 630
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  631 N----GTTALIHAAEKNFLTTVAILLEAGAFVNV----------QQSN----GETALMKACKRGNSDIVRLVIECGAD-- 690
Cdd:TIGR00870 123 SeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADil 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 225543402  691 ------------CNILSKHQNSALYFAKQCnnvlvYELLKSHLE 722
Cdd:TIGR00870 203 tadslgntllhlLVMENEFKAEYEELSCQM-----YNFALSLLD 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 588-714 4.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 588 EEYNLDQEDSTGMTLVMLAAAGGQ-DDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAG-AFVNVQQSN- 664
Cdd:cd22192    6 DELHLLQQKRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSd 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402 665 ---GETALMKACKRGNSDIVRLVIECGADcniLSKHQNSALYFAKQCNNVLVY 714
Cdd:cd22192   86 lyqGETALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFRPGPKNLIYY 135
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
541-722 1.87e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 541 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 620
Cdd:COG0666   64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 621 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 700
Cdd:COG0666  142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                        170       180
                 ....*....|....*....|..
gi 225543402 701 ALYFAKQCNNVLVYELLKSHLE 722
Cdd:COG0666  222 ALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
534-720 3.94e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 3.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 534 MDLQLEWMKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDD 613
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA--DINAKDDGGNTLLHAAARNGDLE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 614 LLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNI 693
Cdd:COG0666  102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                        170       180
                 ....*....|....*....|....*..
gi 225543402 694 LSKHQNSALYFAKQCNNVLVYELLKSH 720
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEA 208
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 7.92e-31

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: 114.69  E-value: 7.92e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225543402  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633    1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
559-718 1.06e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 559 TTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIH 638
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 639 AAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLK 718
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
561-718 1.84e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 561 NRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAA 640
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402 641 EKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV-LVYELLK 718
Cdd:COG0666   96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLeIVKLLLE 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-693 4.67e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  604 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 683
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 225543402  684 VIECGADCNI 693
Cdd:pfam12796  80 LLEKGADINV 89
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 59-108 1.16e-17

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: 77.13  E-value: 1.16e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd00024    1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
560-686 1.04e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 560 TNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 639
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGA--DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 225543402 640 AEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIE 686
Cdd:COG0666  227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
568-661 2.76e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  568 LRDAVKNGDYIAVKVALNsnEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKgAKVNgRQKNGTTALIHAAEKNFLTT 647
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 225543402  648 VAILLEAGAFVNVQ 661
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
636-720 1.17e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  636 LIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECgADCNILSkHQNSALYFAKQCNNVLVYE 715
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*
gi 225543402  716 LLKSH 720
Cdd:pfam12796  79 LLLEK 83
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 1.53e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 65.68  E-value: 1.53e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 225543402   59 FEVERILDMK-CEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRkDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 58-108 3.28e-13

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: 64.78  E-value: 3.28e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225543402  58 VFEVERILDM-KCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18634    1 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 58-106 1.17e-12

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: 63.10  E-value: 1.17e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225543402  58 VFEVERILDM-----KCEGGKNLY-KVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18635    1 EFEVEKLVGIcygdpKKTGERGLYfKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
CHROMO smart00298
Chromatin organization modifier domain;
58-109 3.56e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 61.85  E-value: 3.56e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 225543402    58 VFEVERILDMKCEGGKNL-YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 59-109 4.93e-12

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: 61.37  E-value: 4.93e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402  59 FEVERILDMKC--EGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:cd18632    2 YEVEKIVDEKTdrNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
579-720 4.54e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 579 AVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFV 658
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225543402 659 NVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLKSH 720
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 59-108 9.93e-11

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: 57.49  E-value: 9.93e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18974    1 WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
 59-108 1.53e-10

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: 57.26  E-value: 1.53e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18973    1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ 50
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-106 1.92e-10

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: 56.97  E-value: 1.92e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225543402  58 VFEVERIL------DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18968    1 EYEVEVILaarvvkDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
 59-106 8.78e-10

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: 55.27  E-value: 8.78e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225543402  59 FEVERILDMKCEG---GKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18980    4 YEVEAILDHKVDRryrDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 617-719 1.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 617 LLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSK 696
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                         90       100
                 ....*....|....*....|....
gi 225543402 697 HqnsALYFA-KQCNNVLVYELLKS 719
Cdd:PHA03100 257 T---LLYFKdKDLNTITKIKMLKK 277
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 59-108 1.41e-09

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: 54.37  E-value: 1.41e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18631    2 YVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEFEE 50
Ank_4 pfam13637
Ankyrin repeats (many copies);
632-685 1.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 225543402  632 GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI 685
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 59-106 1.36e-08

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: 51.48  E-value: 1.36e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18650    2 YVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 591-720 1.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 591 NLDQEDSTGMTLVMLAAAGGQDDL--LRLLITKGAKVNGrqkngttalihaaeknfLTTVAILLEAGAFVNVQQSNGETA 668
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTP 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402 669 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA-KQCNNVLVYELLKSH 720
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAiLNNNKEIFKLLLNNG 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 552-725 2.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 552 GEDEPFITTNrIPNNLLrDAVKNGDYIAVKVALNSneeynldqedstGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKN 631
Cdd:PHA02874  58 GADINHINTK-IPHPLL-TAIKIGAHDIIKLLIDN------------GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 632 GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 711
Cdd:PHA02874 124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                        170
                 ....*....|....
gi 225543402 712 LVYELLKSHLETLS 725
Cdd:PHA02874 204 ACIKLLIDHGNHIM 217
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 59-106 4.61e-08

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: 50.01  E-value: 4.61e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18652    2 FVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 59-108 4.90e-08

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: 49.95  E-value: 4.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLE-DCKEVLLEFRK 108
Cdd:cd18638    2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEkSYKEMIDEFEK 52
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 568-732 4.94e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 568 LRDAVKNGDYIAVKVALNSNEEYNlDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTT 647
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 648 VAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQN-SALYFAKQCNNVLVYELLkshletLSR 726
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLF------IKR 224


                 ....*.
gi 225543402 727 VAEETI 732
Cdd:PHA02875 225 GADCNI 230
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 59-106 5.63e-08

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: 49.65  E-value: 5.63e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18653    2 YAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
 59-100 6.25e-08

chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Hypsizygus marmoreus TY3B-I_0 protein, a putative TY3/gypsy retrotransposon polyprotein, and similar proteins. 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: 349326  Cd Length: 49  Bit Score: 49.74  E-value: 6.25e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCK 100
Cdd:cd18970    1 FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 59-108 7.18e-08

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: 49.60  E-value: 7.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18651    2 YVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEFMK 50
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-107 1.05e-07

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: 349322  Cd Length: 49  Bit Score: 48.82  E-value: 1.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDcKEVLLEFR 107
Cdd:cd18966    1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGD-EELLKEWE 48
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 633-772 1.13e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 633 TTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVL 712
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 713 VYELLKSHLETLSRVAEETIRDYFESRLALLEPVfPIACHRlcegPDFSTdfnymPPQNM 772
Cdd:PTZ00322 163 VVQLLSRHSQCHFELGANAKPDSFTGKPPSLEDS-PISSHH----PDFSA-----VPQPM 212
Ank_5 pfam13857
Ankyrin repeats (many copies);
651-705 1.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543402  651 LLEAGAF-VNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA 705
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 58-108 1.86e-07

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: 48.60  E-value: 1.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225543402  58 VFEVERIL-DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18636    1 VYEVEDILaDRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 59-108 2.18e-07

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: 48.28  E-value: 2.18e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEdCKEVLLEFRK 108
Cdd:cd18639    1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLK-CSRLLKQFHK 49
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 56-98 1.01e-06

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 46.30  E-value: 1.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED 98
Cdd:cd18644    1 DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILD 43
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 1.09e-06

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349294  Cd Length: 53  Bit Score: 46.20  E-value: 1.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKK 109
Cdd:cd18647    1 EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPR-LLLAFQKK 53
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
 59-107 1.27e-06

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: 46.32  E-value: 1.27e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402  59 FEVERILDMKCEGGKN----LYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFR 107
Cdd:cd18977    4 YEVEKIVGEKWKKRKNrrvkLYKVRFKGYGPEEDEWLTKEELKNAPEILAEWK 56
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 1.52e-06

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: 45.79  E-value: 1.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543402  59 FEVERIL----DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18964    1 FFVERIIgrrpSARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 580-705 1.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 580 VKVALNSNEEYNLDQEDsTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVN 659
Cdd:PHA02878 150 TKLLLSYGADINMKDRH-KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225543402 660 VQQSNGETALMKACKR-GNSDIVRLVIECGADCNILSKHQN-SALYFA 705
Cdd:PHA02878 229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 613-717 2.34e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 613 DLLRLLITKGAKVNGRQKNGTTAL---IHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNS-DIVRLVIECG 688
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAG 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 225543402 689 ADCNILSKHQNSAL--YFAKQCNNVLVYELL 717
Cdd:PHA03095 108 ADVNAKDKVGRTPLhvYLSGFNINPKVIRLL 138
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 56-106 3.16e-06

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: 45.00  E-value: 3.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPevhLED--CKEVLLEF 106
Cdd:cd18978    1 DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVT---QEDfnDKDMIDEY 50
PTZ00121 PTZ00121
MAEBL; Provisional
 97-470 3.20e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121 1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTL--------KSSRLSGEEKSLKSPDLA 404
Cdd:PTZ00121 1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeakiKAEELKKAEEEKKKVEQL 1638

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402  405 EEEKEKKNEPKGKYQK---RYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 470
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 55-103 4.18e-06

chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 7 (CBX7), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX7 has been shown to function as a tumor suppressor in lung carcinoma and an oncogene in gastric cancer and lymphoma.


Pssm-ID: 349293  Cd Length: 56  Bit Score: 44.69  E-value: 4.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225543402  55 GEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVL 103
Cdd:cd18646    1 GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVM 49
PHA03095 PHA03095
ankyrin-like protein; Provisional
 613-690 5.50e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 613 DLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT---TVAILLEAGAFVNVQQSNGETALMKACKRGNSDI--VRLVIEC 687
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFNInpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDA 176


                 ...
gi 225543402 688 GAD 690
Cdd:PHA03095 177 GAD 179
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 56-108 5.95e-06

chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Coemansia reversa NRRL 1564 SET (Su(var)3-9, enhancer-of-zeste, trithorax) domain-containing protein, and similar proteins. The SU(VAR)3-9 protein is the main chromocenter-specific histone H3-K9 methyltransferase (HMTase) in Drosophila where it plays a role in heterochromatic gene silencing. 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: 349318  Cd Length: 52  Bit Score: 44.10  E-value: 5.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18962    1 EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDL-NDKEILRKYNK 52
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 59-98 6.95e-06

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 43.92  E-value: 6.95e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED 98
Cdd:cd18627    1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILD 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 593-690 1.30e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 593 DQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTA-------------------------------LIHAAE 641
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlwnaisakhhkifrilyhfasisdphaagdlLCTAAK 631

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 225543402 642 KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 690
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PTZ00121 PTZ00121
MAEBL; Provisional
 195-500 1.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  195 FDVKTKKRIWEVKEELK----DSKKPKKDEIKETKELKKANKRAEvrdlkiKIREdVKENRKTKKERYIESPLESEspnd 270
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFgkaeEAKKTETGKAEEARKAEEAKKKAE------DARK-AEEARKAEDARKAEEARKAE---- 1149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  271 slileDDSEDFISDNREENQNV---RSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPK---EIK 344
Cdd:PTZ00121 1150 -----DAKRVEIARKAEDARKAeeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARkaeDAK 1224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  345 KLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEEKEkknepkgkyQKRYDL 424
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK---------KKADEA 1295

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225543402  425 DKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI--SLDSKIMNDNKTKDKCSLKEKRNTRDETDT 500
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
560-669 1.58e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.64  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 560 TNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 639
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGA--DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                         90       100       110
                 ....*....|....*....|....*....|
gi 225543402 640 AEKNFLTTVAILLEAGAFVNVQQSNGETAL 669
Cdd:COG0666  260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 559-685 1.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 559 TTNRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLdqEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIH 638
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 225543402 639 AAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRgNSDIVRLVI 685
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 76-108 2.04e-05

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: 42.66  E-value: 2.04e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 225543402  76 YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18640   20 YLVKWENRSHHENTWEPMANLERCKYLLQMFEK 52
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 591-705 2.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 591 NLDQEDSTGMTLVMLAAAGGQD-DLLRLLITKGAKVNGRQKNGTTALIHAAEKN-FLTTVAILLEAGAFVNVQQSNGETA 668
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTP 378

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 225543402 669 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA 705
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 59-108 2.09e-05

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: 42.50  E-value: 2.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18972    1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK 50
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
 56-108 2.71e-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: 42.51  E-value: 2.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543402  56 EDVFEVERILDMKCEG---GKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18969    1 EEEYEIEEILDVKKGGfedGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEYWK 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 664-693 2.92e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 225543402  664 NGETALMKACKRGNSDIVRLVIECGADCNI 693
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 58-108 3.19e-05

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: 42.16  E-value: 3.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225543402  58 VFEVERILDMKC-EGGKNLYKVRWKGYTSEDDTWEPEVHLEdCKEVLLEFRK 108
Cdd:cd18960    1 VFVVERILDKRLgRNGGEEFLIKWQGFPESDSSWEPRENLQ-CDEMLEEFEK 51
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 59-93 3.39e-05

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL 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: 349331  Cd Length: 49  Bit Score: 41.76  E-value: 3.39e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPE 93
Cdd:cd18975    1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELE 35
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
 59-108 3.60e-05

chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin Organization Modifier (chromo) domain of Caenorhabditis elegans CEC-4, and similar proteins. CEC-4 is a perinuclear heterochromatin anchor, it mediates the anchoring of H3K9 methylation-bearing chromatin at the nuclear periphery in early to mid-stage embryos. It is necessary for anchoring, but does not affect transcriptional repression. CEC-4 contributes to the efficiency with which muscle differentiation is induced following ectopic expression of the master regulator, HLH-1 (MyoD in mammals). 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: 349317  Cd Length: 51  Bit Score: 41.70  E-value: 3.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDT---WEPEvhLEDCKEVLLEFRK 108
Cdd:cd18961    1 YEVEKILSHRIVNGKPLYLVMWVGYPGPVENsemWEED--LKNCGELLKAYKD 51
PTZ00121 PTZ00121
MAEBL; Provisional
 33-499 3.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402   33 AGDEEKDAATKGTVAVGDSEEDGEDVFEVERILDMKC--EGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKKL 110
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE 1299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  111 AENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDT-KEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKDKFKTELEST 189
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  190 SEIIGFDVKTKKRIWEVKEELKDSKKpKKDEIKETKELKK----ANKRAE----VRDLKIKIREDVKENRKTKKERYIES 261
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKK-KADELKKAAAAKKkadeAKKKAEekkkADEAKKKAEEAKKADEAKKKAEEAKK 1458

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  262 PLESESPNDSLILEDDSEDFISDNR--EENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEE 339
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  340 PK---------EIKKLESTNAFLERRAIPKKQR-NQDKGISNLELNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEEKE 409
Cdd:PTZ00121 1539 AKkaeekkkadELKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  410 KKnepkgkyqKRYDLDKEEKARKEPKVLKSF--KEIRNAFDLfkKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCS 487
Cdd:PTZ00121 1619 KI--------KAEELKKAEEEKKKVEQLKKKeaEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                         490
                  ....*....|..
gi 225543402  488 LKEKRNTRDETD 499
Cdd:PTZ00121 1689 KAAEALKKEAEE 1700
Ank_4 pfam13637
Ankyrin repeats (many copies);
599-652 4.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 225543402  599 GMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILL 652
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 55-100 5.40e-05

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 41.63  E-value: 5.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 225543402  55 GEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCK 100
Cdd:cd18649    1 GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDAR 46
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 664-693 5.90e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 5.90e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 225543402   664 NGETALMKACKRGNSDIVRLVIECGADCNI 693
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 613-722 8.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 613 DLLRLLITKGAKVNGRQKNGTTALIHAAE-----KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRG---NSDIVRLV 684
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 225543402 685 IECGADCNILSKHQNSALYFAKQCNNVLVYELLKSHLE 722
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLE 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 560-722 9.28e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  560 TNRIPNNLLRDAVKNGDYIAVKVALnsneeYNLDQEDSTGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQK 630
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  631 N----GTTALIHAAEKNFLTTVAILLEAGAFVNV----------QQSN----GETALMKACKRGNSDIVRLVIECGAD-- 690
Cdd:TIGR00870 123 SeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADil 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 225543402  691 ------------CNILSKHQNSALYFAKQCnnvlvYELLKSHLE 722
Cdd:TIGR00870 203 tadslgntllhlLVMENEFKAEYEELSCQM-----YNFALSLLD 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 594-687 1.68e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 594 QEDSTGMTLVMLA------AAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGET 667
Cdd:PTZ00322  71 EEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                         90       100
                 ....*....|....*....|
gi 225543402 668 ALMKACKRGNSDIVRLVIEC 687
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRH 170
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 58-106 1.71e-04

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: 39.81  E-value: 1.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225543402  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18630    1 EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 664-696 2.34e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 225543402  664 NGETALMKACKR-GNSDIVRLVIECGADCNILSK 696
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 563-722 3.15e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 563 IPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRllITKGAKVnGRQKnGTTALIHAAEK 642
Cdd:PLN03192 493 ILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLK--AKLDPDI-GDSK-GRTPLHIAASK 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 643 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNilSKHQNSALYFAKQCNNV-LVYELLKSHL 721
Cdd:PLN03192 569 GYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLtAMKELLKQGL 646


                 .
gi 225543402 722 E 722
Cdd:PLN03192 647 N 647
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 3.18e-04

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 39.27  E-value: 3.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKK 109
Cdd:cd18645    1 EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPR-LLIAFQNR 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 612-716 3.75e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 612 DDLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT--TVAILLEAGAFVNVQQS-NGETALMKACKrgNSDIVRLVIECG 688
Cdd:PHA02878 214 KPIVHILLENGASTDARDKCGNTPL-HISVGYCKDydILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYG 290

                         90       100       110
                 ....*....|....*....|....*....|....
gi 225543402 689 ADCNILSKHQNSAL------YFAKQCNNVLVYEL 716
Cdd:PHA02878 291 ADINSLNSYKLTPLssavkqYLCINIGRILISNI 324
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
 59-103 5.27e-04

chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a structural and functional homolog of mammalian HP1 (heterochromatin protein 1) and is involved in the chromatin structure by binding to centromeres, telomeres, and the silent mating-type locus. Swi6 contains a N-terminal chromo (CHRromatin Organization MOdifier) domain and a C-terminal chromo shadow domain (CSD). Swi6 binds histone H3 tails methylated at Lys- and the cohesion subunit Psc3, leading to silencing the genes and sister chromatid cohesion. It is also involved in the repression of the silent mating-type loci MAT2 and MAT3. Swi6 may compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. chromodomains mediate the interaction of the heterochromatin with other heterochromatin proteins, thereby affecting chromatin structure (e.g. Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2). CSDs have only been found in proteins that also possess a chromodomain.


Pssm-ID: 349287  Cd Length: 54  Bit Score: 38.64  E-value: 5.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 225543402  59 FEVERILD--MKCEGGKNLYKVRWKGYTSEDD-TWEPEVHLEDCKEVL 103
Cdd:cd18637    2 YVVEKILKhrMARKGGGYEYLLKWEGYDDPSDnTWSSEADCAGCKDLI 49
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 59-100 6.82e-04

chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Magnaporthe grisea putative retrotransposon polyprotein which includes 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: 349327  Cd Length: 50  Bit Score: 38.14  E-value: 6.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 225543402  59 FEVERILDMK---CEGGKNLYKVRWKGYtsEDDTWEPEVHLEDCK 100
Cdd:cd18971    1 YEVEEILAARrrrIRGKGREVLVKWVGY--AEPTWEPLDNLADTA 43
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 9.90e-04

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: 349323  Cd Length: 55  Bit Score: 38.00  E-value: 9.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225543402  59 FEVERIL-----DMKCEGGKN---LYKVRWKGYtsEDDTWEPEVHLEDCKeVLLEFRK 108
Cdd:cd18967    1 WEIEAILahhmsDPRTHPGKPatmLYLTKWEGF--PDETWEPAESFDDRK-ILHDYRR 55
PHA02798 PHA02798
ankyrin-like protein; Provisional
 613-708 1.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 613 DLLRLLITKGAKVNGRQKNGTT---ALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNS---DIVRLVIE 686
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                         90       100
                 ....*....|....*....|..
gi 225543402 687 CGADCNIlskHQNSALYFAKQC 708
Cdd:PHA02798 170 KGVDINT---HNNKEKYDTLHC 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 641-711 1.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225543402 641 EKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 711
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 56-114 2.88e-03

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 36.96  E-value: 2.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKKLAENK 114
Cdd:cd18648    1 ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSR-LIAAFEQKERERE 58
Ank_5 pfam13857
Ankyrin repeats (many copies);
625-669 3.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 225543402  625 VNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETAL 669
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 561-693 3.45e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 561 NRIPNNLLRDAVKNG---DYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDD---LLRLLITKGAKVNGR-QKNGT 633
Cdd:PHA02736  14 DIEGENILHYLCRNGgvtDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKeRVFGN 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225543402 634 TAL-IHAAEKNFltTVAILLEAGAFVNVQQSN--GETALMKACKRGNSDIVRLVIECGADCNI 693
Cdd:PHA02736  94 TPLhIAVYTQNY--ELATWLCNQPGVNMEILNyaFKTPYYVACERHDAKMMNILRAKGAQCKV 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
667-711 3.55e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 225543402  667 TALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 711
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
584-639 3.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543402  584 LNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 639
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 588-714 4.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 588 EEYNLDQEDSTGMTLVMLAAAGGQ-DDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAG-AFVNVQQSN- 664
Cdd:cd22192    6 DELHLLQQKRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSd 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 225543402 665 ---GETALMKACKRGNSDIVRLVIECGADcniLSKHQNSALYFAKQCNNVLVY 714
Cdd:cd22192   86 lyqGETALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFRPGPKNLIYY 135
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
 57-110 6.27e-03

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. 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: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 35.73  E-value: 6.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402  57 DVFEVERILDMK-CEGGKNL-----YKVRWKGYTSEDDTWEPEvhlEDCKEVLLEFRKKL 110
Cdd:cd18663    2 DYVEVDRILDVSvSTDPNTGepvthYLVKWCSLPYEDSTWELE---EDVDPAKIEEFEKL 58
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 611-692 8.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 8.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 611 QDDLL--RLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECG 688
Cdd:PHA02876 155 QDELLiaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234


                 ....
gi 225543402 689 ADCN 692
Cdd:PHA02876 235 SNIN 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 613-755 8.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 8.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 613 DLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAI--LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 690
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225543402 691 CNILSKHQNSALYFA-KQCNNVLVYELLKSHLETlsRVAEETIrDYFESRLALLepvfPIACHRLC 755
Cdd:PHA03095 283 INAVSSDGNTPLSLMvRNNNGRAVRAALAKNPSA--ETVAATL-NTASVAGGDI----PSDATRLC 341
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 202-302 8.64e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 39.45  E-value: 8.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543402 202 RIWEVKEELKDSKKPKKDEIKETKELKK--ANKRAEVRDlkiKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSE 279
Cdd:PRK00247 321 RAPELHAENAEIKKTRTAEKNEAKARKKeiAQKRRAAER---EINREARQERAAAMARARARRAAVKAKKKGLIDASPNE 397

                         90       100
                 ....*....|....*....|...
gi 225543402 280 DFISDNREENQNVRSVRDKTAQE 302
Cdd:PRK00247 398 DTPSENEESKGSPPQVEATTTAE 420
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 61-106 9.50e-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: 35.24  E-value: 9.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 225543402  61 VERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED-CKEVLLEF 106
Cdd:cd18976    3 VESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAY 49
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 616-694 9.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 9.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543402 616 RLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNIL 694
Cdd:PHA02874  19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
 
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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