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Conserved domains on  [gi|1622885384|ref|XP_028693292|]
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M-phase phosphoprotein 8 isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 57-107 2.37e-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: 110.45  E-value: 2.37e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  57 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
542-674 9.86e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 542 MKLEDFQKHLDGKDENFAAADAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQENFLT------------TVAILLEAG 609
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETplhlaayngnleIVKLLLEAG 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384 610 AFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:COG0666   144 ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
PTZ00121 super family cl31754
MAEBL; Provisional
 104-498 1.77e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  104 EFRKKIAENKAKAVRKDiQRLSLNNDIFEANSDSDqqsETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKS 183
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  184 DLESSLESLVFDLRTKKRISEAKEELKESKKpKKDEVKETKELKKvkkgEIRDLKTKTREDPKENRKTKKekcveSQVES 263
Cdd:PTZ00121  1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKK-KADELKKAAAAKK----KADEAKKKAEEKKKADEAKKK-----AEEAK 1444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  264 ESSVLNDSAFPEDDSEGLHSDSrEEKQNTKTARERAGQDIGLEHGFEKPLDSAMSAEEDTDVRGRRKK-KTPRKAEDTR- 341
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKA-EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKk 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  342 --ESRKPENKNAFLEKKTVPKKqRNQDRGKSAAESEKLMPVSAQTPKGwrlSGEERGFWSTDSAEEDK--------ETKK 411
Cdd:PTZ00121  1524 adEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKkaeearieEVMK 1599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  412 TESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKE 491
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679


                   ....*..
gi 1622885384  492 RRNTRDE 498
Cdd:PTZ00121  1680 AKKAEED 1686
 
Name Accession Description Interval E-value
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 57-107 2.37e-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: 110.45  E-value: 2.37e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  57 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
542-674 9.86e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 542 MKLEDFQKHLDGKDENFAAADAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQENFLT------------TVAILLEAG 609
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETplhlaayngnleIVKLLLEAG 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384 610 AFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:COG0666   144 ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
58-108 3.27e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.52  E-value: 3.27e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  58 FEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 108
Cdd:pfam00385   1 YEVERILDHRKdKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
57-108 1.83e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 62.62  E-value: 1.83e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384   57 VFEVEKILDMKTEG-GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 108
Cdd:smart00298   1 EYEVEKILDHRWKKkGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
595-674 1.38e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 595 QENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECgADCNILSkHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:pfam12796   6 KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEK 83
PTZ00121 PTZ00121
MAEBL; Provisional
 104-498 1.77e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  104 EFRKKIAENKAKAVRKDiQRLSLNNDIFEANSDSDqqsETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKS 183
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  184 DLESSLESLVFDLRTKKRISEAKEELKESKKpKKDEVKETKELKKvkkgEIRDLKTKTREDPKENRKTKKekcveSQVES 263
Cdd:PTZ00121  1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKK-KADELKKAAAAKK----KADEAKKKAEEKKKADEAKKK-----AEEAK 1444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  264 ESSVLNDSAFPEDDSEGLHSDSrEEKQNTKTARERAGQDIGLEHGFEKPLDSAMSAEEDTDVRGRRKK-KTPRKAEDTR- 341
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKA-EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKk 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  342 --ESRKPENKNAFLEKKTVPKKqRNQDRGKSAAESEKLMPVSAQTPKGwrlSGEERGFWSTDSAEEDK--------ETKK 411
Cdd:PTZ00121  1524 adEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKkaeearieEVMK 1599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  412 TESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKE 491
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679


                   ....*..
gi 1622885384  492 RRNTRDE 498
Cdd:PTZ00121  1680 AKKAEED 1686
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 602-715 3.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 602 VAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSHLETLSRV 681
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622885384 682 AEETIKDYFEARLALLEPVfPIACHRlcegPDFS 715
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLEDS-PISSHH----PDFS 206
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 181-470 1.92e-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: 48.47  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 181 SKSDLESSLESLVFD-LRTKKRISEAKEELKESKKPKKDEVKE-----------TKELK------KVKKGEIRDLKtktr 242
Cdd:NF033838  119 TKKELDAAFEQFKKDtLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptntykTLELEiaesdvEVKKAELELVK---- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 243 EDPKENRKTKKEKCVESQVESESSvlndsafpeddseglhSDSREEKqnTKTARERAGQDIGLEHGFEkpLDSAMSAEED 322
Cdd:NF033838  195 EEAKEPRDEEKIKQAKAKVESKKA----------------EATRLEK--IKTDREKAEEEAKRRADAK--LKEAVEKNVA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 323 TDVRGRRKKKTPRKA--EDTRESRKPENKN---AFLEKKTVPKKqrNQDRGKSAAESEKlmPVSAQTPKGWRLSGEERGF 397
Cdd:NF033838  255 TSEQDKPKRRAKRGVlgEPATPDKKENDAKssdSSVGEETLPSP--SLKPEKKVAEAEK--KVEEAKKKAKDQKEEDRRN 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 398 WSTDS--------AEEDKETKKTESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIrnAFDLFKLTPEEKNDVSENNRKREE 469
Cdd:NF033838  331 YPTNTyktleleiAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE--ATRLEKIKTDRKKAEEEAKRKAAE 408


                  .
gi 1622885384 470 I 470
Cdd:NF033838  409 E 409
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 618-647 5.77e-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: 5.77e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622885384  618 NGETALMKACKRGNSDIVRLVIECGADCNI 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
189-254 5.08e-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: 5.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622885384 189 LESLVFDLRTK-----KRISEAKEELKESKKPKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE 254
Cdd:COG2433   425 LEAEVEELEAEleekdERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRK 494
 
Name Accession Description Interval E-value
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 57-107 2.37e-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: 110.45  E-value: 2.37e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  57 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 58-107 1.30e-18

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: 79.83  E-value: 1.30e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd00024     1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
542-674 9.86e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 542 MKLEDFQKHLDGKDENFAAADAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQENFLT------------TVAILLEAG 609
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETplhlaayngnleIVKLLLEAG 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384 610 AFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:COG0666   144 ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
595-698 2.28e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 595 QENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          90       100
                  ....*....|....*....|....
gi 1622885384 675 LETLSRVAEETIKDYFEARLALLE 698
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
505-665 5.68e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 5.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 505 IAAEGDQEGSDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAAADAIPSNVLRDAVKNGDYITVKVA 584
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 585 LNSNEEYNLDQENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNN 664
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165


                  .
gi 1622885384 665 V 665
Cdd:COG0666   166 L 166
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
58-108 3.27e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.52  E-value: 3.27e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  58 FEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 108
Cdd:pfam00385   1 YEVERILDHRKdKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 57-107 4.17e-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: 64.39  E-value: 4.17e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  57 VFEVEKILDM-KTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18634     1 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 58-108 1.35e-12

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


Pssm-ID: 349282  Cd Length: 55  Bit Score: 62.91  E-value: 1.35e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384  58 FEVEKILDMKT--EGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 108
Cdd:cd18632     2 YEVEKIVDEKTdrNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
CHROMO smart00298
Chromatin organization modifier domain;
57-108 1.83e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 62.62  E-value: 1.83e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384   57 VFEVEKILDMKTEG-GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKK 108
Cdd:smart00298   1 EYEVEKILDHRWKKkGELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 57-105 2.34e-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: 62.33  E-value: 2.34e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384  57 VFEVEKILDM------KTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 105
Cdd:cd18635     1 EFEVEKLVGIcygdpkKTGERGLYFKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
Ank_2 pfam12796
Ankyrin repeats (3 copies);
595-674 1.38e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 595 QENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECgADCNILSkHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:pfam12796   6 KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEK 83
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 57-105 5.32e-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: 58.51  E-value: 5.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384  57 VFEVEKIL------DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 105
Cdd:cd18968     1 EYEVEVILaarvvkDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 58-107 2.46e-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: 56.29  E-value: 2.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 107
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 ...
 58-107 6.75e-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: 55.33  E-value: 6.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18973     1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ 50
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 58-105 9.45e-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: 54.65  E-value: 9.45e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 105
Cdd:cd18653     2 YAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-647 1.03e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 569 LRDAVKNGDYITVKVALNSNEEYNLDQENFLT------------TVAILLEaGAFVNVQqSNGETALMKACKRGNSDIVR 636
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTalhlaaknghleIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1622885384 637 LVIECGADCNI 647
Cdd:pfam12796  79 LLLEKGADINV 89
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 58-105 1.04e-09

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: 54.57  E-value: 1.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 105
Cdd:cd18650     2 YVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
PTZ00121 PTZ00121
MAEBL; Provisional
 104-498 1.77e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  104 EFRKKIAENKAKAVRKDiQRLSLNNDIFEANSDSDqqsETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKS 183
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  184 DLESSLESLVFDLRTKKRISEAKEELKESKKpKKDEVKETKELKKvkkgEIRDLKTKTREDPKENRKTKKekcveSQVES 263
Cdd:PTZ00121  1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKK-KADELKKAAAAKK----KADEAKKKAEEKKKADEAKKK-----AEEAK 1444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  264 ESSVLNDSAFPEDDSEGLHSDSrEEKQNTKTARERAGQDIGLEHGFEKPLDSAMSAEEDTDVRGRRKK-KTPRKAEDTR- 341
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKA-EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKk 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  342 --ESRKPENKNAFLEKKTVPKKqRNQDRGKSAAESEKLMPVSAQTPKGwrlSGEERGFWSTDSAEEDK--------ETKK 411
Cdd:PTZ00121  1524 adEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKkaeearieEVMK 1599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  412 TESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKE 491
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679


                   ....*..
gi 1622885384  492 RRNTRDE 498
Cdd:PTZ00121  1680 AKKAEED 1686
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 58-105 3.11e-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: 3.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEF 105
Cdd:cd18652     2 FVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
 58-105 4.86e-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: 52.96  E-value: 4.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  58 FEVEKILDMKTEG---GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 105
Cdd:cd18980     4 YEVEAILDHKVDRryrDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 58-107 4.86e-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: 52.87  E-value: 4.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18974     1 WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
537-674 7.68e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 7.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 537 LQLEWMKLEDFQKHLDGKDENFAAADAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQENFLTTVAILLEAGAFVNVQQ 616
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622885384 617 SNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_5 pfam13857
Ankyrin repeats (many copies);
605-659 9.26e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 9.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622885384 605 LLEAGAF-VNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA 659
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 58-107 1.28e-08

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


Pssm-ID: 349298  Cd Length: 50  Bit Score: 51.53  E-value: 1.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 107
Cdd:cd18651     2 YVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEFMK 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 602-715 3.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 602 VAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSHLETLSRV 681
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622885384 682 AEETIKDYFEARLALLEPVfPIACHRlcegPDFS 715
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLEDS-PISSHH----PDFS 206
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-106 6.42e-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: 49.59  E-value: 6.42e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDcKEVLLEFR 106
Cdd:cd18966     1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGD-EELLKEWE 48
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
560-672 6.86e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 6.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 560 AADAIPSNVLRDAVKNGDYITVKV---------ALNSNEEYNLD---QENFLTTVAILLEAGAFVNVQQSNGETALMKAC 627
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLlleagadvnARDNDGETPLHlaaENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622885384 628 KRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLK 672
Cdd:COG0666   228 ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
PTZ00121 PTZ00121
MAEBL; Provisional
 104-549 7.48e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 7.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  104 EFRKKIAENKAKAVRKDIQRLSLNNDIFEANSDSDQQSETKEDTSPKKKKKKLR---QREEKSPDDLKKKKAKAGKLKDK 180
Cdd:PTZ00121  1216 EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEA 1295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  181 SKSDLESSLESLVFDLRTKKRISEAKEELKESKKpKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE--KCVE 258
Cdd:PTZ00121  1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEKAEaaEKKK 1373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  259 SQVESESSVLNDSAFPEDDSEGLHSDSREEKQNTKTARERAGQDiglehgfEKPLDSAMSAEEDTDVRGRRKKKTPRKAE 338
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK-------KKADEAKKKAEEKKKADEAKKKAEEAKKA 1446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  339 DTRESRKPENKNAFLEKKTVPKKQRNQDRGKSAAESEKLMPVSAQTPKGWRLSGEERgfwstDSAEEDKETKKTESKEKY 418
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-----KAAEAKKKADEAKKAEEA 1521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  419 QKRHDSDKEEKGRKEPKgLKTLKEIRNAFDLFKL----TPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRN 494
Cdd:PTZ00121  1522 KKADEAKKAEEAKKADE-AKKAEEKKKADELKKAeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622885384  495 TRDETDTWAYiAAEGDQEGSDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQK 549
Cdd:PTZ00121  1601 YEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
 58-99 8.44e-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: 8.44e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCK 99
Cdd:cd18970     1 FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 55-97 1.25e-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: 1.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED 97
Cdd:cd18644     1 DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILD 43
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 58-107 1.65e-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: 48.41  E-value: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLE-DCKEVLLEFRK 107
Cdd:cd18638     2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEkSYKEMIDEFEK 52
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 597-691 2.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 597 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSHle 676
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN-- 247

                          90
                  ....*....|....*
gi 1622885384 677 tlsRVAEETIKDYFE 691
Cdd:PHA03100  248 ---GPSIKTIIETLL 259
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 58-107 2.26e-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: 47.90  E-value: 2.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEdCKEVLLEFRK 107
Cdd:cd18639     1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLK-CSRLLKQFHK 49
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 55-108 4.35e-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: 47.36  E-value: 4.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKK 108
Cdd:cd18647     1 EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPR-LLLAFQKK 53
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 55-107 1.41e-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: 46.02  E-value: 1.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLeDCKEVLLEFRK 107
Cdd:cd18962     1 EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDL-NDKEILRKYNK 52
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 54-102 1.55e-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: 45.85  E-value: 1.55e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622885384  54 GEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVL 102
Cdd:cd18646     1 GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVM 49
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 58-97 1.92e-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: 1.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED 97
Cdd:cd18627     1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILD 40
Ank_2 pfam12796
Ankyrin repeats (3 copies);
623-698 2.22e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 623 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSHLETLSRVAEET------IKDYFEARLAL 696
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTalhyaaRSGHLEIVKLL 80


                  ..
gi 1622885384 697 LE 698
Cdd:pfam12796  81 LE 82
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
 58-107 2.48e-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: 45.17  E-value: 2.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGY---TSDDDTWEPEihLEDCKEVLLEFRK 107
Cdd:cd18961     1 YEVEKILSHRIVNGKPLYLVMWVGYpgpVENSEMWEED--LKNCGELLKAYKD 51
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 55-105 2.70e-06

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


Pssm-ID: 349334  Cd Length: 52  Bit Score: 45.00  E-value: 2.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPeihLED--CKEVLLEF 105
Cdd:cd18978     1 DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVT---QEDfnDKDMIDEY 50
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-107 3.45e-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: 44.63  E-value: 3.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622885384  58 FEVEKIL----DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18964     1 FFVERIIgrrpSARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK 54
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
 58-106 8.02e-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: 8.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622885384  58 FEVEKILDMKTEGGK----VLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFR 106
Cdd:cd18977     4 YEVEKIVGEKWKKRKnrrvKLYKVRFKGYGPEEDEWLTKEELKNAPEILAEWK 56
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 57-107 1.32e-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: 43.21  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  57 VFEVEKIL-DMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18636     1 VYEVEDILaDRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 58-92 1.67e-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: 1.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPE 92
Cdd:cd18975     1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELE 35
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
 55-107 1.86e-05

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


Pssm-ID: 349325  Cd Length: 56  Bit Score: 42.90  E-value: 1.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622885384  55 EDVFEVEKILDMKTEG---GKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18969     1 EEEYEIEEILDVKKGGfedGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEYWK 56
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 181-470 1.92e-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: 48.47  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 181 SKSDLESSLESLVFD-LRTKKRISEAKEELKESKKPKKDEVKE-----------TKELK------KVKKGEIRDLKtktr 242
Cdd:NF033838  119 TKKELDAAFEQFKKDtLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptntykTLELEiaesdvEVKKAELELVK---- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 243 EDPKENRKTKKEKCVESQVESESSvlndsafpeddseglhSDSREEKqnTKTARERAGQDIGLEHGFEkpLDSAMSAEED 322
Cdd:NF033838  195 EEAKEPRDEEKIKQAKAKVESKKA----------------EATRLEK--IKTDREKAEEEAKRRADAK--LKEAVEKNVA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 323 TDVRGRRKKKTPRKA--EDTRESRKPENKN---AFLEKKTVPKKqrNQDRGKSAAESEKlmPVSAQTPKGWRLSGEERGF 397
Cdd:NF033838  255 TSEQDKPKRRAKRGVlgEPATPDKKENDAKssdSSVGEETLPSP--SLKPEKKVAEAEK--KVEEAKKKAKDQKEEDRRN 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 398 WSTDS--------AEEDKETKKTESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIrnAFDLFKLTPEEKNDVSENNRKREE 469
Cdd:NF033838  331 YPTNTyktleleiAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE--ATRLEKIKTDRKKAEEEAKRKAAE 408


                  .
gi 1622885384 470 I 470
Cdd:NF033838  409 E 409
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 595-681 2.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 595 QENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVlvyDLLKSH 674
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI---DTIKAI 230


                  ....*..
gi 1622885384 675 LETLSRV 681
Cdd:PHA02876  231 IDNRSNI 237
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 562-659 2.65e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 562 DAIPSNVLRDAVKNGDYITVKVALNSNEEYNLD------------QENFLTTVAILLEAGAFVNVQQSNGETALMKACKR 629
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEddngcypihiaiKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622885384 630 GNSDIVRLVIECGADCNILSKHQNSALHFA 659
Cdd:PHA02874  201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 618-647 2.85e-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: 2.85e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622885384 618 NGETALMKACKRGNSDIVRLVIECGADCNI 647
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
599-639 3.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622885384 599 LTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI 639
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 199-493 4.51e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  199 KKRISEAKEELKESKKPKK-DEVKETKELKKVKKGEIRDLKTKTREDPK--ENRKTKKEKCVES--QVESESSVLNDSAF 273
Cdd:PTZ00121  1165 KAEEARKAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEERKaeEARKAEDAKKAEAvkKAEEAKKDAEEAKK 1244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  274 PEDDSEGLHSDSREEKQNTKTARERAgqdiglehgfekpldsAMSAEEDTDVRGRRKKKTPRKAEdtrESRKPENKNAFL 353
Cdd:PTZ00121  1245 AEEERNNEEIRKFEEARMAHFARRQA----------------AIKAEEARKADELKKAEEKKKAD---EAKKAEEKKKAD 1305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  354 EKKTVPKKQRNQDRGKSAAESEKLMPVSAQtpkgwRLSGEERGFWSTDSAEEDKETKKTESKEKYQKRHDSDKEEKGRKE 433
Cdd:PTZ00121  1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAK-----KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622885384  434 PKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIP----LDFKTIDDHKTKENKQSLKERR 493
Cdd:PTZ00121  1381 DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeAKKKAEEKKKADEAKKKAEEAK 1444
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 57-107 4.77e-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: 41.39  E-value: 4.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  57 VFEVEKILDMKT-EGGKVLYKVRWKGYTSDDDTWEPEIHLEdCKEVLLEFRK 107
Cdd:cd18960     1 VFVVERILDKRLgRNGGEEFLIKWQGFPESDSSWEPRENLQ-CDEMLEEFEK 51
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 54-99 5.60e-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: 5.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622885384  54 GEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCK 99
Cdd:cd18649     1 GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDAR 46
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 618-647 5.77e-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: 5.77e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622885384  618 NGETALMKACKRGNSDIVRLVIECGADCNI 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-107 6.86e-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: 41.08  E-value: 6.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622885384  58 FEVEKIL-----DMKTEGGK---VLYKVRWKGYtsDDDTWEPEIHLEDCKeVLLEFRK 107
Cdd:cd18967     1 WEIEAILahhmsDPRTHPGKpatMLYLTKWEGF--PDETWEPAESFDDRK-ILHDYRR 55
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 58-99 6.86e-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: 40.84  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622885384  58 FEVEKILDMKT---EGGKVLYKVRWKGYtsDDDTWEPEIHLEDCK 99
Cdd:cd18971     1 YEVEEILAARRrriRGKGREVLVKWVGY--AEPTWEPLDNLADTA 43
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 58-107 7.28e-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: 41.12  E-value: 7.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622885384  58 FEVEKILDMKTEGGKVL--YKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18640     1 EPVEKIVAKRFNPRKKTweYLVKWENRSHHENTWEPMANLERCKYLLQMFEK 52
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 58-107 1.00e-04

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: 40.58  E-value: 1.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622885384  58 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRK 107
Cdd:cd18972     1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK 50
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 564-690 1.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 564 IPsNVLRDAVKNGDYITVKVALNSNEEYNL----DQENflTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI 639
Cdd:PHA02874   68 IP-HPLLTAIKIGAHDIIKLLIDNGVDTSIlpipCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622885384 640 ECGADCNILSKHQNSALHFAKQSNNvlvYDLLKSHLEtlsRVAEETIKDYF 690
Cdd:PHA02874  145 EYGADVNIEDDNGCYPIHIAIKHNF---FDIIKLLLE---KGAYANVKDNN 189
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 55-108 1.71e-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: 40.04  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKK 108
Cdd:cd18645     1 EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPR-LLIAFQNR 53
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
 58-102 2.11e-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: 39.80  E-value: 2.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622885384  58 FEVEKILD--MKTEGGKVLYKVRWKGY-TSDDDTWEPEIHLEDCKEVL 102
Cdd:cd18637     2 YVVEKILKhrMARKGGGYEYLLKWEGYdDPSDNTWSSEADCAGCKDLI 49
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 60-105 2.15e-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: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622885384  60 VEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLED-CKEVLLEF 105
Cdd:cd18976     3 VESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAY 49
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 57-105 2.25e-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: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622885384  57 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEF 105
Cdd:cd18630     1 EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 618-650 2.29e-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: 2.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622885384 618 NGETALMKACKR-GNSDIVRLVIECGADCNILSK 650
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 605-676 3.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 3.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622885384 605 LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAkqSNNVLVYDLLKSHLE 676
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILKLLLE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 602-657 3.66e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 3.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622885384 602 VAILLEAGAFVNVQQSNGETALMKACKRGNS-DIVRLVIECGADCNILSKHQNSALH 657
Cdd:PHA03095   66 VRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH 122
Ank_4 pfam13637
Ankyrin repeats (many copies);
621-665 4.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622885384 621 TALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNV 665
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 595-679 8.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 595 QENFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKSH 674
Cdd:PHA02874  133 KKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212


                  ....*
gi 1622885384 675 LETLS 679
Cdd:PHA02874  213 GNHIM 217
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 569-678 8.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 569 LRDAV------KNGDYITVKVALNSNEEYNLDQENFLTTVAILLEAGAFVN-VQQSNGETALMKACKRGNSDIVRLVIEC 641
Cdd:PHA02875   45 FRDSEaikllmKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIAR 124

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622885384 642 GADCNILSKHQNSALHFAKQSNNVLVYDLLKSHLETL 678
Cdd:PHA02875  125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
PTZ00121 PTZ00121
MAEBL; Provisional
 217-525 1.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  217 KDEVKETKELKKVKKGEIRDLKTKTredpKENRKTKKEKCVESQVESESSVLNDSAfpEDDSEGLHSDSREEKQNTKTAR 296
Cdd:PTZ00121  1052 IDGNHEGKAEAKAHVGQDEGLKPSY----KDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAE 1125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  297 ERAGQDIGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDTR---ESRKPENKNAFLEKKTVPKKQRNQDRGKSAA- 372
Cdd:PTZ00121  1126 DARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARkaeDAKKAEAARKAEEVRKAEELRKAEDARKAEAa 1205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  373 ---ESEKLMPVSAQTPKGWRLSGEERGFWSTDSAEEDKETKKTESKEKYQK-----------RHDSDKEEKGRKEPKgLK 438
Cdd:PTZ00121  1206 rkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeearmahfarRQAAIKAEEARKADE-LK 1284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  439 TLKEIRNAFDLFKltPEEKNDVSENNRKREEIpldfKTIDDHKTK--ENKQSLKERRNTRDETDTWAYIAAEGDQEGSDS 516
Cdd:PTZ00121  1285 KAEEKKKADEAKK--AEEKKKADEAKKKAEEA----KKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358


                   ....*....
gi 1622885384  517 VCQADENSD 525
Cdd:PTZ00121  1359 AEAAEEKAE 1367
PTZ00121 PTZ00121
MAEBL; Provisional
 96-562 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384   96 EDCKEVLLEFRKKIAENKAKAVRKDIQRLSLNNDIFEAnsDSDQQSETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAG 175
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  176 KLKDKSKSDLESSLESLVFDlrtKKRISEAKEELKESKKPKKDEVKETKElKKVKKGEIRDLKTKTREDPKENRKTKKEK 255
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  256 CVESQVESESsvlndsafpEDDSEGLHSDSREEKQNTKTAREragqdiglehgfekpLDSAMSAEEDTDVRGRRKKKTPR 335
Cdd:PTZ00121  1647 KKAEELKKAE---------EENKIKAAEEAKKAEEDKKKAEE---------------AKKAEEDEKKAAEALKKEAEEAK 1702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  336 KAEDTRESRKPENKNAFLEKKTVPKKQRNQDRGKSAAESEKLMPVSAQTPKgwrlsGEERGFWSTDSAEEDKETKKTESK 415
Cdd:PTZ00121  1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEK 1777

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384  416 EKYQKRHDSDKEEKGRKEPKglKTLKEIRNAFDlfkltpeeknDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNT 495
Cdd:PTZ00121  1778 EAVIEEELDEEDEKRRMEVD--KKIKDIFDNFA----------NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622885384  496 RDETDTWAY----IAAEGDQEGSDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAAAD 562
Cdd:PTZ00121  1846 ADAFEKHKFnknnENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIID 1916
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 55-113 1.36e-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: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622885384  55 EDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKeVLLEFRKKIAENK 113
Cdd:cd18648     1 ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSR-LIAAFEQKERERE 58
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 602-672 1.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622885384 602 VAILLEAGAFVNVQQSN-GETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFA-KQSNNVLVYDLLK 672
Cdd:PHA02878  150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAvKHYNKPIVHILLE 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 585-665 3.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 585 LNSNEEYNLdqENFLTTVAILLEAGAFVNVQQSNGETALMKA--CKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQS 662
Cdd:PHA03100   74 YLSNIKYNL--TDVKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLES 151


                  ...
gi 1622885384 663 NNV 665
Cdd:PHA03100  152 NKI 154
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
189-254 5.08e-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: 5.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622885384 189 LESLVFDLRTK-----KRISEAKEELKESKKPKKDEVKETKELKKvKKGEIRDLKTKTREDPKENRKTKKE 254
Cdd:COG2433   425 LEAEVEELEAEleekdERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRK 494
PHA03095 PHA03095
ankyrin-like protein; Provisional
 602-672 9.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 9.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622885384 602 VAILLEAGAFVNVQQSNGETALmKACKRG---NSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVyDLLK 672
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANV-ELLR 171
PHA02798 PHA02798
ankyrin-like protein; Provisional
 594-676 9.68e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622885384 594 DQENFLTTVAILLEAGAFVNVQQSNGETALMKACKRG---NSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDL 670
Cdd:PHA02798   84 DYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEI 163


                  ....*.
gi 1622885384 671 LKSHLE 676
Cdd:PHA02798  164 IKLLLE 169
 
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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