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Conserved domains on  [gi|41055989|ref|NP_059990|]
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M-phase phosphoprotein 8 [Homo sapiens]

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];
485-746 6.80e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 6.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 485 ENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAATDA 564
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 565 IPSNVLRDAVKNGDYITVKVALNSNEeyNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEK 644
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 645 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLE 724
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                       250       260
                ....*....|....*....|..
gi 41055989 725 TLSRVAEETIKDYFEARLALLE 746
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAA 265
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.57e-29

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: 111.22  E-value: 1.57e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  58 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18633   1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PTZ00121 super family cl31754
MAEBL; Provisional
 200-550 3.05e-07

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   200 KKRISEAKEELKESKKpKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE--KFVESQVESESSVLNDSPFPED 277
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKK-KADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   278 DSEGLHSDSREEKQNTKSARERAGQDMGLEHgFEKPLDSAMSAEEdtdvrGRRKKKTPRKAEDTR----ENRKLEN-KNA 352
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADE-----AKKKAEEAKKADEAKkkaeEAKKAEEaKKK 1465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   353 FLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERglwstDSAEEDKETKRNESKEKYQKRHDSDKEEKGR 432
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK-----KKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   433 KEPKgLKTLKEIRNAFDLFKltPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQ 512
Cdd:PTZ00121 1541 KAEE-KKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 41055989   513 EVLDSVcQADENSDGRQQILSLGMDLQLEWMKLEDFQK 550
Cdd:PTZ00121 1618 AKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
485-746 6.80e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 6.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 485 ENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAATDA 564
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 565 IPSNVLRDAVKNGDYITVKVALNSNEeyNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEK 644
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 645 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLE 724
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                       250       260
                ....*....|....*....|..
gi 41055989 725 TLSRVAEETIKDYFEARLALLE 746
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAA 265
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.57e-29

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: 111.22  E-value: 1.57e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  58 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18633   1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
606-695 4.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   606 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 685
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 41055989   686 VIECGADCNI 695
Cdd:pfam12796  80 LLEKGADINV 89
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 2.34e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 2.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41055989    59 FEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRKdKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
58-109 1.39e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 63.00  E-value: 1.39e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41055989     58 VFEVEKILDMKTEG-GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKkGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 575-739 9.12e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 9.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  575 KNGDYITVKVALNSNEEYNLDqeDSSGMTLVMLAAAGGQDDL--LRLLITKGAKVNGrqkngttalihaaeknfLTTVAI 652
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANVNIK--NSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  653 LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHletlsRVAEE 732
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN-----GPSIK 252


                 ....*..
gi 41055989  733 TIKDYFE 739
Cdd:PHA03100 253 TIIETLL 259
PTZ00121 PTZ00121
MAEBL; Provisional
 200-550 3.05e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   200 KKRISEAKEELKESKKpKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE--KFVESQVESESSVLNDSPFPED 277
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKK-KADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   278 DSEGLHSDSREEKQNTKSARERAGQDMGLEHgFEKPLDSAMSAEEdtdvrGRRKKKTPRKAEDTR----ENRKLEN-KNA 352
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADE-----AKKKAEEAKKADEAKkkaeEAKKAEEaKKK 1465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   353 FLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERglwstDSAEEDKETKRNESKEKYQKRHDSDKEEKGR 432
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK-----KKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   433 KEPKgLKTLKEIRNAFDLFKltPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQ 512
Cdd:PTZ00121 1541 KAEE-KKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 41055989   513 EVLDSVcQADENSDGRQQILSLGMDLQLEWMKLEDFQK 550
Cdd:PTZ00121 1618 AKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 666-695 5.91e-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: 5.91e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 41055989    666 NGETALMKACKRGNSDIVRLVIECGADCNI 695
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 182-420 8.77e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 46.16  E-value: 8.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  182 SKPDLESSLESLVFD-LRTKKRISEAKEELKESKKPKKDEVKE-----------TKELK------KVKKGEIRDLKtktr 243
Cdd:NF033838 119 TKKELDAAFEQFKKDtLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptntykTLELEiaesdvEVKKAELELVK---- 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  244 EDPKENRKTKKEKFVESQVESESSvlndspfpeddseglhSDSREEKqnTKSARERAGQDMGLEHGFEkpLDSAMSAEED 323
Cdd:NF033838 195 EEAKEPRDEEKIKQAKAKVESKKA----------------EATRLEK--IKTDREKAEEEAKRRADAK--LKEAVEKNVA 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  324 TDVRGRRKKKTPRKAedtrenrklenknafLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDS 403
Cdd:NF033838 255 TSEQDKPKRRAKRGV---------------LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKK 319

                        250
                 ....*....|....*...
gi 41055989  404 AEEDK-ETKRNESKEKYQ 420
Cdd:NF033838 320 AKDQKeEDRRNYPTNTYK 337
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 593-724 7.39e-04

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: 43.15  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   593 NLDQEDSSGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQKN----GTTALIHAAEKNFLTTVAILLEAGAF 659
Cdd:TIGR00870  74 NLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   660 VNV----------QQSN----GETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA------KQSNNVLV---Y 716
Cdd:TIGR00870 154 VPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefKAEYEELScqmY 233


                  ....*...
gi 41055989   717 DLLKNHLE 724
Cdd:TIGR00870 234 NFALSLLD 241
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 182-530 3.61e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    182 SKPDLESSLESLVFDLRTKKRISEAKEELKESKKPKKDEVKETKELKKvkkgeIRDLKTKTREDPKENRKTKKEKFVESQ 261
Cdd:pfam02463  150 MKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-----QELKLKEQAKKALEYYQLKEKLELEEE 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    262 VESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDT 341
Cdd:pfam02463  225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    342 RENRK-LENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEErglwSTDSAEEDKETKRNESKEKYQ 420
Cdd:pfam02463  305 LERRKvDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE----ELEKLQEKLEQLEEELLAKKK 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    421 KRHDSDKEEKGRKEPKGLKTLKEIRNA------FDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERR 494
Cdd:pfam02463  381 LESERLSSAAKLKEEELELKSEEEKEAqlllelARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 41055989    495 NTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQ 530
Cdd:pfam02463  461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
190-255 5.65e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 5.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055989 190 LESLVFDLRTK-----KRISEAKEELKESKKPKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE 255
Cdd:COG2433 425 LEAEVEELEAEleekdERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRK 494
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
485-746 6.80e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 6.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 485 ENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAATDA 564
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 565 IPSNVLRDAVKNGDYITVKVALNSNEeyNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEK 644
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 645 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLE 724
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                       250       260
                ....*....|....*....|..
gi 41055989 725 TLSRVAEETIKDYFEARLALLE 746
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAA 265
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.57e-29

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: 111.22  E-value: 1.57e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  58 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18633   1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
561-723 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 41055989 561 ATDAIPSNVLRDAVKNGDYITVKVALNSNEeyNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIH 640
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 641 AAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLK 720
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272


                ...
gi 41055989 721 NHL 723
Cdd:COG0666 273 LAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
548-721 1.85e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 1.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 548 FQKHLDGKDENFAATDAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKV 627
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 628 NGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA 707
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                       170
                ....*....|....*
gi 41055989 708 KQSNNV-LVYDLLKN 721
Cdd:COG0666 161 AANGNLeIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
606-695 4.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   606 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 685
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 41055989   686 VIECGADCNI 695
Cdd:pfam12796  80 LLEKGADINV 89
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 59-108 8.68e-19

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: 80.60  E-value: 8.68e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd00024   1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
Ank_2 pfam12796
Ankyrin repeats (3 copies);
570-663 3.02e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   570 LRDAVKNGDYITVKVALNsnEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKgAKVNgRQKNGTTALIHAAEKNFLTT 649
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 41055989   650 VAILLEAGAFVNVQ 663
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-736 3.67e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   638 LIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECgADCNILSkHQNSALHFAKQSNNVLVYD 717
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*....
gi 41055989   718 LLknhletLSRVAEETIKD 736
Cdd:pfam12796  79 LL------LEKGADINVKD 91
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 2.34e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 2.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41055989    59 FEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRKdKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 58-108 3.26e-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: 3.26e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055989  58 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18634   1 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 59-109 8.77e-13

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: 63.68  E-value: 8.77e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055989  59 FEVEKILDMKT--EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 109
Cdd:cd18632   2 YEVEKIVDEKTdrNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
CHROMO smart00298
Chromatin organization modifier domain;
58-109 1.39e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 63.00  E-value: 1.39e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41055989     58 VFEVEKILDMKTEG-GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKkGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 58-106 1.40e-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: 1.40e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055989  58 VFEVEKILDM-----KTEGGKVLY-KVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 106
Cdd:cd18635   1 EFEVEKLVGIcygdpKKTGERGLYfKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
583-722 1.15e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 583 KVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNV 662
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 663 QQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNH 722
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-106 2.62e-11

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: 59.28  E-value: 2.62e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055989  58 VFEVEKIL------DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 106
Cdd:cd18968   1 EYEVEVILaarvvkDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 575-739 9.12e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 9.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  575 KNGDYITVKVALNSNEEYNLDqeDSSGMTLVMLAAAGGQDDL--LRLLITKGAKVNGrqkngttalihaaeknfLTTVAI 652
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANVNIK--NSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  653 LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHletlsRVAEE 732
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN-----GPSIK 252


                 ....*..
gi 41055989  733 TIKDYFE 739
Cdd:PHA03100 253 TIIETLL 259
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 59-108 1.86e-10

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: 56.68  E-value: 1.86e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 108
Cdd:cd18631   2 YVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEFEE 50
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
 59-108 4.32e-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: 55.72  E-value: 4.32e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18973   1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ 50
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 59-106 8.87e-10

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: 55.04  E-value: 8.87e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 106
Cdd:cd18653   2 YAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 59-106 8.98e-10

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: 54.95  E-value: 8.98e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 106
Cdd:cd18650   2 YVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 59-106 2.52e-09

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: 53.47  E-value: 2.52e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 106
Cdd:cd18652   2 FVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 59-108 3.50e-09

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: 53.25  E-value: 3.50e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18974   1 WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
 59-106 3.82e-09

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: 53.34  E-value: 3.82e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  59 FEVEKILDMKTEG---GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 106
Cdd:cd18980   4 YEVEAILDHKVDRryrDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-707 9.49e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 9.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055989   653 LLEAGAF-VNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA 707
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 59-108 9.95e-09

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: 51.92  E-value: 9.95e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 108
Cdd:cd18651   2 YVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEFMK 50
Ank_4 pfam13637
Ankyrin repeats (many copies);
634-687 1.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41055989   634 GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI 687
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 613-727 1.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  613 QDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 692
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41055989  693 CNILSKHQNSALHFAKQSNNVLVYDLLKNHLETLS 727
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
 556-720 2.18e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  556 DENFAATDAIPSNVLRDAVKNGDYITVK-----VALNSNEEYNlDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGR 630
Cdd:PHA03095   1 DEEDESVDIIMEAALYDYLLNASNVTVEevrrlLAAGADVNFR-GEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  631 QKNGTTALIHAAE-KNFLTTVAILLEAGAFVNVQQSNGETALmKACKRG---NSDIVRLVIECGADCNILSKHQNSALHF 706
Cdd:PHA03095  80 ERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAV 158

                        170
                 ....*....|....
gi 41055989  707 AKQSNNVLVyDLLK 720
Cdd:PHA03095 159 LLKSRNANV-ELLR 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 615-724 2.47e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKN-GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADC 693
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110
                 ....*....|....*....|....*....|.
gi 41055989  694 NILSKHQNSALHFAkqSNNVLVYDLLKNHLE 724
Cdd:PHA02878 228 DARDKCGNTPLHIS--VGYCKDYDILKLLLE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 581-721 2.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  581 TVKVALNSNEEYNLdqEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFV 660
Cdd:PHA02874 106 MIKTILDCGIDVNI--KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055989  661 NVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKN 721
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 570-734 4.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  570 LRDAVKNGDYITVKVALNSNEEYNlDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTT 649
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  650 VAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQN-SALHFAKQSNNVLVYDLLknhletLSR 728
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLF------IKR 224


                 ....*.
gi 41055989  729 VAEETI 734
Cdd:PHA02875 225 GADCNI 230
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-107 4.45e-08

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: 49.97  E-value: 4.45e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDcKEVLLEFR 107
Cdd:cd18966   1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGD-EELLKEWE 48
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 582-714 4.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  582 VKVALNSNEEYNLDQEDSsGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVN 661
Cdd:PHA02878 150 TKLLLSYGADINMKDRHK-GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41055989  662 VQQSNGETALMKACKR-GNSDIVRLVIECGADCNILSKHQN-SALHFAKQSNNVL 714
Cdd:PHA02878 229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERKL 283
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 635-763 6.52e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  635 TTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVL 714
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 41055989  715 VYDLLKNHLETLSRVAEETIKDYFEARLALLEPVfPIACHRlcegPDFS 763
Cdd:PTZ00322 163 VVQLLSRHSQCHFELGANAKPDSFTGKPPSLEDS-PISSHH----PDFS 206
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
 59-100 8.83e-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: 49.36  E-value: 8.83e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCK 100
Cdd:cd18970   1 FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 56-98 1.19e-07

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: 49.00  E-value: 1.19e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED 98
Cdd:cd18644   1 DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILD 43
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 59-108 1.33e-07

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: 48.79  E-value: 1.33e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLE-DCKEVLLEFRK 108
Cdd:cd18638   2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEkSYKEMIDEFEK 52
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 59-108 1.55e-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: 48.67  E-value: 1.55e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEdCKEVLLEFRK 108
Cdd:cd18639   1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLK-CSRLLKQFHK 49
PTZ00121 PTZ00121
MAEBL; Provisional
 200-550 3.05e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   200 KKRISEAKEELKESKKpKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE--KFVESQVESESSVLNDSPFPED 277
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKK-KADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   278 DSEGLHSDSREEKQNTKSARERAGQDMGLEHgFEKPLDSAMSAEEdtdvrGRRKKKTPRKAEDTR----ENRKLEN-KNA 352
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADE-----AKKKAEEAKKADEAKkkaeEAKKAEEaKKK 1465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   353 FLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERglwstDSAEEDKETKRNESKEKYQKRHDSDKEEKGR 432
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK-----KKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   433 KEPKgLKTLKEIRNAFDLFKltPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQ 512
Cdd:PTZ00121 1541 KAEE-KKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 41055989   513 EVLDSVcQADENSDGRQQILSLGMDLQLEWMKLEDFQK 550
Cdd:PTZ00121 1618 AKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 3.66e-07

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: 47.74  E-value: 3.66e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKK 109
Cdd:cd18647   1 EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPR-LLLAFQKK 53
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 55-103 1.04e-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: 46.62  E-value: 1.04e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41055989  55 GEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVL 103
Cdd:cd18646   1 GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVM 49
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 56-108 1.06e-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: 46.41  E-value: 1.06e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 108
Cdd:cd18962   1 EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDL-NDKEILRKYNK 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 593-710 1.13e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  593 NLDQEDSSGMT-LVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT---TVAILLEAGAFVNVQQSNGE 668
Cdd:PHA03095  75 DVNAPERCGFTpLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFNInpkVIRLLLRKGADVNALDLYGM 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 41055989  669 TALMKACKRGNSDI--VRLVIECGADCNILSKHQNSALHFAKQS 710
Cdd:PHA03095 154 TPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQS 197
PTZ00121 PTZ00121
MAEBL; Provisional
 105-470 1.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   105 EFRKKIAENKAKAvrkdiqrlslnNDIFEANSDSDQQSETKEDTSPKKKKKKLRQREE---KSPDDLKKKKAKAGKLKDK 181
Cdd:PTZ00121 1395 EAKKKAEEDKKKA-----------DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKAEEAK 1463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   182 SKPDLESSLESLVFDLRTKKRISEAKEELKESKKpKKDEVKETKELKKvKKGEIRDLKTKTREDpkENRKTKKEKFVESQ 261
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKK-KADEAKKAEEAKKAD--EAKKAEEAKKADEA 1539

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   262 VESESSVLNDSPFPEDDSEglhsDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKtprKAEDT 341
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM---KAEEA 1612

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   342 RENRKLENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDKETKRNESKEKYQK 421
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 41055989   422 RHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREE 470
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 59-98 1.70e-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: 45.46  E-value: 1.70e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED 98
Cdd:cd18627   1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILD 40
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
 59-108 1.73e-06

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: 45.56  E-value: 1.73e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGY---TSDDDTWEPEihLEDCKEVLLEFRK 108
Cdd:cd18961   1 YEVEKILSHRIVNGKPLYLVMWVGYpgpVENSEMWEED--LKNCGELLKAYKD 51
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 593-712 1.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  593 NLDQEDSSGMTLVMLAAAGGQD-DLLRLLITKGAKVNGRQKNGTTALIHAAE-KNFLTTVAILLEAGAFVNVQQSNGETA 670
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41055989  671 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNN 712
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN 420
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 56-106 2.25e-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: 45.38  E-value: 2.25e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPeihLED--CKEVLLEF 106
Cdd:cd18978   1 DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVT---QEDfnDKDMIDEY 50
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 2.63e-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: 45.02  E-value: 2.63e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055989  59 FEVEKIL----DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18964   1 FFVERIIgrrpSARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 615-724 5.07e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.83  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKNGTTALIHAAE-----KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRG---NSDIVRLV 686
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 41055989  687 IECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLE 724
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLE 169
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
 59-107 7.24e-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: 44.01  E-value: 7.24e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055989  59 FEVEKILDMKTEGGK----VLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFR 107
Cdd:cd18977   4 YEVEKIVGEKWKKRKnrrvKLYKVRFKGYGPEEDEWLTKEELKNAPEILAEWK 56
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 58-108 1.11e-05

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: 43.59  E-value: 1.11e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055989  58 VFEVEKIL-DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18636   1 VYEVEDILaDRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
 56-108 1.37e-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: 43.28  E-value: 1.37e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055989  56 EDVFEVEKILDMKTEG---GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18969   1 EEEYEIEEILDVKKGGfedGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEYWK 56
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 59-93 1.52e-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: 42.92  E-value: 1.52e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPE 93
Cdd:cd18975   1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELE 35
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 554-707 1.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  554 GKDENFAATDAIpsNVLRDAVKNGDYITVKVALNSNEeyNLDQEDssgmtLVMLAAAGGQD-DLLRLLITKGAKVNGRQK 632
Cdd:PHA02876 201 GADVNIIALDDL--SVLECAVDSKNIDTIKAIIDNRS--NINKND-----LSLLKAIRNEDlETSLLLYDAGFSVNSIDD 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055989  633 NGTTALIHAAEKNFLTT-VAILLEAGAFVNVQQSNGETALMKACKRG-NSDIVRLVIECGADCNILSKHQNSALHFA 707
Cdd:PHA02876 272 CKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 595-692 1.92e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  595 DQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTA-------------------------------LIHAAE 643
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlwnaisakhhkifrilyhfasisdphaagdlLCTAAK 631

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 41055989  644 KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 692
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
570-671 2.37e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 570 LRDAVKNGDYITVKVALNSNEeyNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTT 649
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGA--DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                        90       100
                ....*....|....*....|..
gi 41055989 650 VAILLEAGAFVNVQQSNGETAL 671
Cdd:COG0666 268 VKLLLLALLLLAAALLDLLTLL 289
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 666-695 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 41055989   666 NGETALMKACKRGNSDIVRLVIECGADCNI 695
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 3.67e-05

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: 41.85  E-value: 3.67e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41055989  59 FEVEKIL-----DMKTEGGK---VLYKVRWKGYtsDDDTWEPEIHLEDCKeVLLEFRK 108
Cdd:cd18967   1 WEIEAILahhmsDPRTHPGKpatMLYLTKWEGF--PDETWEPAESFDDRK-ILHDYRR 55
PTZ00121 PTZ00121
MAEBL; Provisional
 200-494 3.70e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   200 KKRISEAKEELKESKKPKK-DEVKETKELKKVKKGEIRDLKTKTREDPK--ENRKTKKEKFVESQVESESSvlndspfpE 276
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEA--------K 1236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   277 DDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDTRENRKLEnKNAFLEK 356
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK-KKAEEAK 1315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   357 KTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDKETKRNESKEKYQKRHDSDKEEKGRKEPK 436
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055989   437 GLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEI----PLDFKTIDDHKTKENKQSLKERR 494
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKAEEAK 1457
Ank_4 pfam13637
Ankyrin repeats (many copies);
601-654 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41055989   601 GMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILL 654
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 58-108 4.26e-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: 41.78  E-value: 4.26e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055989  58 VFEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEdCKEVLLEFRK 108
Cdd:cd18960   1 VFVVERILDKRLgRNGGEEFLIKWQGFPESDSSWEPRENLQ-CDEMLEEFEK 51
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 59-108 4.99e-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: 41.51  E-value: 4.99e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055989  59 FEVEKILDMKTEGGKVL--YKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18640   1 EPVEKIVAKRFNPRKKTweYLVKWENRSHHENTWEPMANLERCKYLLQMFEK 52
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 55-100 5.68e-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: 5.68e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 41055989  55 GEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCK 100
Cdd:cd18649   1 GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDAR 46
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 666-695 5.91e-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: 5.91e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 41055989    666 NGETALMKACKRGNSDIVRLVIECGADCNI 695
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 59-100 6.83e-05

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: 41.22  E-value: 6.83e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 41055989  59 FEVEKILDMKT---EGGKVLYKVRWKGYtsDDDTWEPEIHLEDCK 100
Cdd:cd18971   1 YEVEEILAARRrriRGKGREVLVKWVGY--AEPTWEPLDNLADTA 43
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 59-108 7.96e-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: 40.96  E-value: 7.96e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41055989  59 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 108
Cdd:cd18972   1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK 50
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 182-420 8.77e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 46.16  E-value: 8.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  182 SKPDLESSLESLVFD-LRTKKRISEAKEELKESKKPKKDEVKE-----------TKELK------KVKKGEIRDLKtktr 243
Cdd:NF033838 119 TKKELDAAFEQFKKDtLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptntykTLELEiaesdvEVKKAELELVK---- 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  244 EDPKENRKTKKEKFVESQVESESSvlndspfpeddseglhSDSREEKqnTKSARERAGQDMGLEHGFEkpLDSAMSAEED 323
Cdd:NF033838 195 EEAKEPRDEEKIKQAKAKVESKKA----------------EATRLEK--IKTDREKAEEEAKRRADAK--LKEAVEKNVA 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  324 TDVRGRRKKKTPRKAedtrenrklenknafLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDS 403
Cdd:NF033838 255 TSEQDKPKRRAKRGV---------------LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKK 319

                        250
                 ....*....|....*...
gi 41055989  404 AEEDK-ETKRNESKEKYQ 420
Cdd:NF033838 320 AKDQKeEDRRNYPTNTYK 337
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 197-425 1.25e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 45.81  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   197 LRTKKRISEAKEELKESKKPKKDEVKETKELKKVKKGEIRDLKTKTREDPKENRKTKKEKFVESQVESESSVLNDSPFPE 276
Cdd:PTZ00108 1153 AKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQK 1232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   277 DDSEGLHSDSREEKQNTKS-----ARERAGQDMGLEHGFEKPLDSAMSA----EEDTDVRGRRKKKTPRKAEDTREN--R 345
Cdd:PTZ00108 1233 TKPKKSSVKRLKSKKNNSSkssedNDEFSSDDLSKEGKPKNAPKRVSAVqyspPPPSKRPDGESNGGSKPSSPTKKKvkK 1312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   346 KLENKNAFLEKKTvPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEErglwSTDSAEED-KETKRNESKEKYQKRHD 424
Cdd:PTZ00108 1313 RLEGSLAALKKKK-KSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKS----DSSSEDDDdSEVDDSEDEDDEDDEDD 1387


                  .
gi 41055989   425 S 425
Cdd:PTZ00108 1388 D 1388
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 596-689 1.36e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  596 QEDSSGMTLVMLA------AAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGET 669
Cdd:PTZ00322  71 EEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                         90       100
                 ....*....|....*....|
gi 41055989  670 ALMKACKRGNSDIVRLVIEC 689
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRH 170
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 1.59e-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: 40.43  E-value: 1.59e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKK 109
Cdd:cd18645   1 EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPR-LLIAFQNR 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 643-713 1.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055989  643 EKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNV 713
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
 59-103 1.76e-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: 40.19  E-value: 1.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 41055989  59 FEVEKILD--MKTEGGKVLYKVRWKGY-TSDDDTWEPEIHLEDCKEVL 103
Cdd:cd18637   2 YVVEKILKhrMARKGGGYEYLLKWEGYdDPSDNTWSSEADCAGCKDLI 49
PHA02798 PHA02798
ankyrin-like protein; Provisional
 615-720 2.04e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKNGTT---ALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNS---DIVRLVIE 688
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                         90       100       110
                 ....*....|....*....|....*....|....
gi 41055989  689 CGADCNILS-KHQNSALH-FAKQSNNVLVYDLLK 720
Cdd:PHA02798 170 KGVDINTHNnKEKYDTLHcYFKYNIDRIDADILK 203
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 58-106 2.13e-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: 2.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41055989  58 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 106
Cdd:cd18630   1 EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 61-106 2.17e-04

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: 39.86  E-value: 2.17e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 41055989  61 VEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED-CKEVLLEF 106
Cdd:cd18976   3 VESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAY 49
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 666-698 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 41055989   666 NGETALMKACKR-GNSDIVRLVIECGADCNILSK 698
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 620-728 2.48e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  620 LITKGAKVNGRQKNGTTALIHAAEKNFLT-TVAILLEAGAFVNVQQSNGETALMKACKRG-NSDIVRLVIECGADCNILS 697
Cdd:PHA02876 293 LLERGADVNAKNIKGETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARD 372

                         90       100       110
                 ....*....|....*....|....*....|....
gi 41055989  698 KHQNSALHFAKQSNNVLVYDLLKNH---LETLSR 728
Cdd:PHA02876 373 YCDKTPIHYAAVRNNVVIINTLLDYgadIEALSQ 406
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 614-729 3.48e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  614 DDLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT--TVAILLEAGAFVNVQQS-NGETALMKACKrgNSDIVRLVIECG 690
Cdd:PHA02878 214 KPIVHILLENGASTDARDKCGNTPL-HISVGYCKDydILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYG 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 41055989  691 ADCNILSKHQNSALHFA-KQSNNVLVYDLLKNHLETLSRV 729
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAvKQYLCINIGRILISNICLLKRI 330
Ank_4 pfam13637
Ankyrin repeats (many copies);
669-713 4.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 41055989   669 TALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNV 713
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 564-694 4.75e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  564 AIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRllITKGAKVnGRQKnGTTALIHAAE 643
Cdd:PLN03192 492 VILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLK--AKLDPDI-GDSK-GRTPLHIAAS 567

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  644 KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCN 694
Cdd:PLN03192 568 KGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 593-724 7.39e-04

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: 43.15  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   593 NLDQEDSSGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQKN----GTTALIHAAEKNFLTTVAILLEAGAF 659
Cdd:TIGR00870  74 NLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   660 VNV----------QQSN----GETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA------KQSNNVLV---Y 716
Cdd:TIGR00870 154 VPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefKAEYEELScqmY 233


                  ....*...
gi 41055989   717 DLLKNHLE 724
Cdd:TIGR00870 234 NFALSLLD 241
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 572-722 8.69e-04

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: 43.15  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   572 DAVKNGDYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQ-DDLLRLLITKGAKVN-GRqkngttALIHAAEKNFLTT 649
Cdd:TIGR00870  23 PAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAvGD------TLLHAISLEYVDA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   650 V--AILLEAGAF--------VNVQQSN----GETALMKACKRGNSDIVRLVIECGADCNI--------LSKHQNSALH-- 705
Cdd:TIGR00870  97 VeaILLHLLAAFrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvKSQGVDSFYHge 176

                         170       180
                  ....*....|....*....|.
gi 41055989   706 ----FAKQSNNVLVYDLLKNH 722
Cdd:TIGR00870 177 splnAAACLGSPSIVALLSED 197
PTZ00121 PTZ00121
MAEBL; Provisional
 218-512 1.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   218 KDEVKETKELKKVKKGEIRDLKTKTredpKENRKTKKEKFVESQVESESSVLndspfpEDDSEGLHSDSREEKQNTKSAR 297
Cdd:PTZ00121 1052 IDGNHEGKAEAKAHVGQDEGLKPSY----KDFDFDAKEDNRADEATEEAFGK------AEEAKKTETGKAEEARKAEEAK 1121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   298 ERAGQDMGLEHGFE----KPLDSAMSAEEDTDVRGRRKKKTPRKAEDTR---ENRKLENKNAFLEKKTVPKKQRNQDRSK 370
Cdd:PTZ00121 1122 KKAEDARKAEEARKaedaRKAEEARKAEDAKRVEIARKAEDARKAEEARkaeDAKKAEAARKAEEVRKAEELRKAEDARK 1201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   371 SAA----ELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDK---ETKRNESKEKYQ--------KRHDSDKEEKGRKEP 435
Cdd:PTZ00121 1202 AEAarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaeEERNNEEIRKFEearmahfaRRQAAIKAEEARKAD 1281

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055989   436 KgLKTLKEIRNAFDLFKltPEEKNDVSENNRKREEipldfktidDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQ 512
Cdd:PTZ00121 1282 E-LKKAEEKKKADEAKK--AEEKKKADEAKKKAEE---------AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 56-114 1.20e-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: 37.73  E-value: 1.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055989  56 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKKIAENK 114
Cdd:cd18648   1 ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSR-LIAAFEQKERERE 58
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 568-695 1.69e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  568 NVLRDAVKNG---DYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDD---LLRLLITKGAKVNGR-QKNGTTAL-I 639
Cdd:PHA02736  19 NILHYLCRNGgvtDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKeRVFGNTPLhI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41055989  640 HAAEKNFltTVAILLEAGAFVNVQQSN--GETALMKACKRGNSDIVRLVIECGADCNI 695
Cdd:PHA02736  99 AVYTQNY--ELATWLCNQPGVNMEILNyaFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 188-498 2.43e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   188 SSLESLVFDLRTKKRISEA--KEELKESKKPKKDEVketKELKKVKKGEIRDLKTKTREDPKENRKTKK-EKFVESQVES 264
Cdd:PTZ00108 1002 GKLERELARLSNKVRFIKHviNGELVITNAKKKDLV---KELKKLGYVRFKDIIKKKSEKITAEEEEGAeEDDEADDEDD 1078

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   265 ESSVLNDSPF-----------PEDDSEGLHSDSREEKQNTKSARERAGQDMGLE--HGFEKPLDSAMSAEEDTDVRGRRK 331
Cdd:PTZ00108 1079 EEELGAAVSYdyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLEdlDKFEEALEEQEEVEEKEIAKEQRL 1158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   332 KKTPRKAEDTRENRKLENKNAFLEKKTVPKKQ-------RNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSA 404
Cdd:PTZ00108 1159 KSKTKGKASKLRKPKLKKKEKKKKKSSADKSKkasvvgnSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKS 1238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989   405 EEDKETKRNESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIrNAFDLFKLTPEEKNDVSENN---RKREEIPLDFKTIDDH 481
Cdd:PTZ00108 1239 SVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRV-SAVQYSPPPPSKRPDGESNGgskPSSPTKKKVKKRLEGS 1317

                         330
                  ....*....|....*..
gi 41055989   482 KTKENKQSLKERRNTRD 498
Cdd:PTZ00108 1318 LAALKKKKKSEKKTARK 1334
Ank_5 pfam13857
Ankyrin repeats (many copies);
586-641 2.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055989   586 LNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 641
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
627-671 3.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 41055989   627 VNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETAL 671
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
614-722 3.31e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989 614 DDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADC 693
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100
                ....*....|....*....|....*....
gi 41055989 694 NILSKHQNSALHFAKQSNNVLVYDLLKNH 722
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 182-530 3.61e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    182 SKPDLESSLESLVFDLRTKKRISEAKEELKESKKPKKDEVKETKELKKvkkgeIRDLKTKTREDPKENRKTKKEKFVESQ 261
Cdd:pfam02463  150 MKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-----QELKLKEQAKKALEYYQLKEKLELEEE 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    262 VESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDT 341
Cdd:pfam02463  225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    342 RENRK-LENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEErglwSTDSAEEDKETKRNESKEKYQ 420
Cdd:pfam02463  305 LERRKvDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE----ELEKLQEKLEQLEEELLAKKK 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989    421 KRHDSDKEEKGRKEPKGLKTLKEIRNA------FDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERR 494
Cdd:pfam02463  381 LESERLSSAAKLKEEELELKSEEEKEAqlllelARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 41055989    495 NTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQ 530
Cdd:pfam02463  461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 613-717 5.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  613 QDDLL--RLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECG 690
Cdd:PHA02876 155 QDELLiaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                         90       100
                 ....*....|....*....|....*..
gi 41055989  691 ADCNILSKHQNSALHFAKQSNNVLVYD 717
Cdd:PHA02876 235 SNINKNDLSLLKAIRNEDLETSLLLYD 261
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 618-719 5.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  618 RLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI---------- 687
Cdd:PHA02874  19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilp 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 41055989  688 -------------ECGADCNILSKHQNSALHFAKQSNNVLVYDLL 719
Cdd:PHA02874  99 ipciekdmiktilDCGIDVNIKDAELKTFLHYAIKKGDLESIKML 143
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
190-255 5.65e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 5.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055989 190 LESLVFDLRTK-----KRISEAKEELKESKKPKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE 255
Cdd:COG2433 425 LEAEVEELEAEleekdERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRK 494
PHA03095 PHA03095
ankyrin-like protein; Provisional
 615-757 6.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAI--LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 692
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055989  693 CNILSKHQNSALHFAKQSNNvlvYDLLKNHLETlsRVAEETIKDYFEaRLALLEPVFPIACHRLC 757
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNNN---GRAVRAALAK--NPSAETVAATLN-TASVAGGDIPSDATRLC 341
PHA03095 PHA03095
ankyrin-like protein; Provisional
 615-705 8.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 8.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKNGTTALiHAAEKNF---LTTVAILLEAGAFVNVQQSNGETAL--MKACKRGNSDIVRLVIEC 689
Cdd:PHA03095 133 KVIRLLLRKGADVNALDLYGMTPL-AVLLKSRnanVELLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRA 211

                         90
                 ....*....|....*.
gi 41055989  690 GADCNILSKHQNSALH 705
Cdd:PHA03095 212 GCDPAATDMLGNTPLH 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 615-744 8.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055989  615 DLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKA-CKRGNSDIVRLVIECGADC 693
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANV 435

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41055989  694 NILSKHQNSALHFAKQSNNVLvyDLLKNHLETLSRVAEETIKDYFEARLAL 744
Cdd:PHA02876 436 NSKNKDLSTPLHYACKKNCKL--DVIEMLLDNGADVNAINIQNQYPLLIAL 484
CD2_cpSRP43_like cd18629
chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
 60-96 9.18e-03

chromodomain 2 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 2 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349279  Cd Length: 48  Bit Score: 35.17  E-value: 9.18e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 41055989  60 EVEKILDMKTEGGKVLYKVRWKgyTSDDDTWEPEIHL 96
Cdd:cd18629   4 EVNEILESRGKGKDMEYLIEWK--DGGDCEWVKGVHV 38
 
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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