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Conserved domains on  [gi|604824794|gb|JAC34734|]
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hypothetical protein [Amblyomma triste]

Protein Classification

chromo domain-containing protein( domain architecture ID 13035978)

chromo (chromatin organization modifier) domain-containing protein may bind methylated histone tails

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 11-59 1.75e-31

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: 115.95  E-value: 1.75e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18627    1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILDPRLLAAFES 49
CBX7_C pfam17218
CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It ...
 553-584 1.28e-10

CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It is bound by the RAWUL domain of the RING1B protein.


:

Pssm-ID: 465385  Cd Length: 33  Bit Score: 56.47  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 604824794  553 DFWQKQSPVVDQVLITDVTANLVTVTVRECRT 584
Cdd:pfam17218   1 EYWRPSPAPPDKVVVTDVTANSLTVTFRECST 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 104-552 2.07e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  104 APATPHGNSSSTETNSAMSPPHSPPPTLSP-----APAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKpQPAEA 178
Cdd:PHA03247 2492 AGAAPDPGGGGPPDPDAPPAPSRLAPAILPdepvgEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-RSVPP 2570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  179 KEPAAKP-KPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPePVTAPVLKPNQAADVSPSCSPPV 257
Cdd:PHA03247 2571 PRPAPRPsEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-PPPSPSPAANEPDPHPPPTVPPP 2649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  258 LESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMqmhQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPH 337
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA---RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  338 FMNGSAPVARAPFARPPVTFKPISP--RLAVSVSQQPHAVHHSHPPASHLAVPPVAA-RLGTGQLGPATVARISRPPTHL 414
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPggPARPARPPTTAGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDPAD 2806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  415 VTSAVPSNATSAPSSqvvANSAGPNPSPTVAT-IVPVNTPAPPNPAHATTGQAPPqhNGPPPTATPVVPNGRESAAPHHg 493
Cdd:PHA03247 2807 PPAAVLAPAAALPPA---ASPAGPLPPPTSAQpTAPPPPPGPPPPSLPLGGSVAP--GGDVRRRPPSRSPAAKPAAPAR- 2880

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 604824794  494 ggndrenvckPAVSAVSQGKPLHSHNGQAASPPTLLPPKEANAEPATAEPEYSPMAIIP 552
Cdd:PHA03247 2881 ----------PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
 
Name Accession Description Interval E-value
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 11-59 1.75e-31

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: 115.95  E-value: 1.75e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18627    1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILDPRLLAAFES 49
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
11-60 7.77e-16

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 71.84  E-value: 7.77e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 604824794   11 FAAENIQKKRIRKGRV-EYLVKWRGWSHKYNTWEPEENILDV-RLLEAFESS 60
Cdd:pfam00385   1 YEVERILDHRKDKGGKeEYLVKWKGYPYDENTWEPEENLSKCpELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
10-58 3.14e-14

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 67.24  E-value: 3.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 604824794    10 VFAAENIQKKR-IRKGRVEYLVKWRGWSHKYNTWEPEENILDV-RLLEAFE 58
Cdd:smart00298   1 EYEVEKILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENLLNCsKKLDNYK 51
CBX7_C pfam17218
CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It ...
 553-584 1.28e-10

CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It is bound by the RAWUL domain of the RING1B protein.


Pssm-ID: 465385  Cd Length: 33  Bit Score: 56.47  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 604824794  553 DFWQKQSPVVDQVLITDVTANLVTVTVRECRT 584
Cdd:pfam17218   1 EYWRPSPAPPDKVVVTDVTANSLTVTFRECST 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 104-552 2.07e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  104 APATPHGNSSSTETNSAMSPPHSPPPTLSP-----APAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKpQPAEA 178
Cdd:PHA03247 2492 AGAAPDPGGGGPPDPDAPPAPSRLAPAILPdepvgEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-RSVPP 2570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  179 KEPAAKP-KPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPePVTAPVLKPNQAADVSPSCSPPV 257
Cdd:PHA03247 2571 PRPAPRPsEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-PPPSPSPAANEPDPHPPPTVPPP 2649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  258 LESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMqmhQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPH 337
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA---RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  338 FMNGSAPVARAPFARPPVTFKPISP--RLAVSVSQQPHAVHHSHPPASHLAVPPVAA-RLGTGQLGPATVARISRPPTHL 414
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPggPARPARPPTTAGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDPAD 2806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  415 VTSAVPSNATSAPSSqvvANSAGPNPSPTVAT-IVPVNTPAPPNPAHATTGQAPPqhNGPPPTATPVVPNGRESAAPHHg 493
Cdd:PHA03247 2807 PPAAVLAPAAALPPA---ASPAGPLPPPTSAQpTAPPPPPGPPPPSLPLGGSVAP--GGDVRRRPPSRSPAAKPAAPAR- 2880

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 604824794  494 ggndrenvckPAVSAVSQGKPLHSHNGQAASPPTLLPPKEANAEPATAEPEYSPMAIIP 552
Cdd:PHA03247 2881 ----------PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-555 7.19e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 39.51  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  175 PAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTgPAPPEKDPEP-VTAPVlkPNQAADVSPSC 253
Cdd:pfam05109 466 PTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTT-PTPNATSPTPaVTTPT--PNATSPTLGKT 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  254 SPPVLESSKKPDTTGsaatkrkfearPLHMTSSPQQIPVPPAMQmHQPPPSKMPRLTRPADVPPVAATVPRpppvvaaTS 333
Cdd:pfam05109 543 SPTSAVTTPTPNATS-----------PTPAVTTPTPNATIPTLG-KTSPTSAVTTPTPNATSPTVGETSPQ-------AN 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  334 TAPHFMNG--SAPVARAP--FARPPVTF--KPISPRLAVSVSQQPHAVHHSHPPA------SHLAVPPVAARLGTGQLGP 401
Cdd:pfam05109 604 TTNHTLGGtsSTPVVTSPpkNATSAVTTgqHNITSSSTSSMSLRPSSISETLSPStsdnstSHMPLLTSAHPTGGENITQ 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  402 ATVARISrppTHLVTSAVPsnatsAPSSQVVANSAGPNPSPTVATIVPVNTPAPPNPAHATTGQAPPQHNGPPPTATPVV 481
Cdd:pfam05109 684 VTPASTS---THHVSTSSP-----APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTG 755

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  482 PNGRESAAPHHGGGNDRENVCKPAVS-AVSQGKPLHSHNGQAASPP----------TLLPPKEANAE-----PATAEPEY 545
Cdd:pfam05109 756 GKANSTTGGKHTTGHGARTSTEPTTDyGGDSTTPRTRYNATTYLPPstssklrprwTFTSPPVTTAQatvpvPPTSQPRF 835

                         410
                  ....*....|
gi 604824794  546 SPMAIIPDFW 555
Cdd:pfam05109 836 SNLSMLVLQW 845
 
Name Accession Description Interval E-value
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 11-59 1.75e-31

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: 115.95  E-value: 1.75e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18627    1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILDPRLLAAFES 49
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 8-61 6.21e-28

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: 106.01  E-value: 6.21e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFESSQ 61
Cdd:cd18644    1 DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILDRRLIEIFERTN 54
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 8-63 1.31e-25

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: 99.74  E-value: 1.31e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFESSQKD 63
Cdd:cd18648    1 ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERE 56
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 8-62 2.40e-25

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: 98.98  E-value: 2.40e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFESSQK 62
Cdd:cd18645    1 EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRER 55
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 7-59 2.41e-25

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: 99.02  E-value: 2.41e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 604824794   7 GERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18649    1 GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDARLLAAFEE 53
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 8-58 1.23e-22

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: 91.27  E-value: 1.23e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFE 58
Cdd:cd18647    1 EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQ 51
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 7-62 5.92e-20

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: 83.60  E-value: 5.92e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 604824794   7 GERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFESSQK 62
Cdd:cd18646    1 GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEE 56
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 11-59 4.26e-17

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 75.21  E-value: 4.26e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVR-LLEAFES 59
Cdd:cd00024    1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPeLIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
11-60 7.77e-16

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 71.84  E-value: 7.77e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 604824794   11 FAAENIQKKRIRKGRV-EYLVKWRGWSHKYNTWEPEENILDV-RLLEAFESS 60
Cdd:pfam00385   1 YEVERILDHRKDKGGKeEYLVKWKGYPYDENTWEPEENLSKCpELIEEFKDR 52
chromodomain cd18963
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 8-76 1.06e-14

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: 349319  Cd Length: 57  Bit Score: 68.49  E-value: 1.06e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKyntwepeenildvrlleafESSQKDSGPGKRGHKSKKE 76
Cdd:cd18963    1 ERVFAAECIIKRRVRKGRIEYLVKWKGWASK-------------------ERERELYGPKKRGPKPKKF 50
CHROMO smart00298
Chromatin organization modifier domain;
10-58 3.14e-14

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 67.24  E-value: 3.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 604824794    10 VFAAENIQKKR-IRKGRVEYLVKWRGWSHKYNTWEPEENILDV-RLLEAFE 58
Cdd:smart00298   1 EYEVEKILDHRwKKKGELEYLVKWKGYSYSEDTWEPEENLLNCsKKLDNYK 51
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 11-58 3.52e-13

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: 64.00  E-value: 3.52e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFE 58
Cdd:cd18631    2 YVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENLDCPDLIAEFE 49
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 11-59 2.09e-12

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: 61.97  E-value: 2.09e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18653    2 YAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENLDCQDLIQQYEA 50
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 8-57 3.50e-12

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: 61.59  E-value: 3.50e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDV-RLLEAF 57
Cdd:cd18968    5 EVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCdDLLERF 55
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 11-48 1.75e-11

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: 59.19  E-value: 1.75e-11
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENI 48
Cdd:cd18650    2 YVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENL 39
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 11-57 4.25e-11

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: 58.08  E-value: 4.25e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAF 57
Cdd:cd18651    2 YVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEF 48
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 11-48 8.00e-11

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: 57.65  E-value: 8.00e-11
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENI 48
Cdd:cd18638    2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNL 39
CBX7_C pfam17218
CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It ...
 553-584 1.28e-10

CBX family C-terminal motif; This motif is found at the C-terminus of CBX family proteins. It is bound by the RAWUL domain of the RING1B protein.


Pssm-ID: 465385  Cd Length: 33  Bit Score: 56.47  E-value: 1.28e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 604824794  553 DFWQKQSPVVDQVLITDVTANLVTVTVRECRT 584
Cdd:pfam17218   1 EYWRPSPAPPDKVVVTDVTANSLTVTFRECST 32
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 11-57 1.73e-10

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: 56.55  E-value: 1.73e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAF 57
Cdd:cd18652    2 FVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAF 48
PHA03247 PHA03247
large tegument protein UL36; Provisional
 104-552 2.07e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  104 APATPHGNSSSTETNSAMSPPHSPPPTLSP-----APAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKpQPAEA 178
Cdd:PHA03247 2492 AGAAPDPGGGGPPDPDAPPAPSRLAPAILPdepvgEPVHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-RSVPP 2570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  179 KEPAAKP-KPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPePVTAPVLKPNQAADVSPSCSPPV 257
Cdd:PHA03247 2571 PRPAPRPsEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-PPPSPSPAANEPDPHPPPTVPPP 2649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  258 LESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMqmhQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPH 337
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA---RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  338 FMNGSAPVARAPFARPPVTFKPISP--RLAVSVSQQPHAVHHSHPPASHLAVPPVAA-RLGTGQLGPATVARISRPPTHL 414
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPggPARPARPPTTAGPPAPAPPAAPAAGPPRRLtRPAVASLSESRESLPSPWDPAD 2806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  415 VTSAVPSNATSAPSSqvvANSAGPNPSPTVAT-IVPVNTPAPPNPAHATTGQAPPqhNGPPPTATPVVPNGRESAAPHHg 493
Cdd:PHA03247 2807 PPAAVLAPAAALPPA---ASPAGPLPPPTSAQpTAPPPPPGPPPPSLPLGGSVAP--GGDVRRRPPSRSPAAKPAAPAR- 2880

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 604824794  494 ggndrenvckPAVSAVSQGKPLHSHNGQAASPPTLLPPKEANAEPATAEPEYSPMAIIP 552
Cdd:PHA03247 2881 ----------PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 11-57 2.55e-10

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: 56.01  E-value: 2.55e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAF 57
Cdd:cd18975    1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELEDNIKNPRLIEEF 47
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 8-58 4.55e-10

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: 55.09  E-value: 4.55e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794   8 ERVFAAENiqkKRIRKGRVEYLVKWRGWSHKynTWEPEENILDVRLLEAFE 58
Cdd:cd18971    4 EEILAARR---RRIRGKGREVLVKWVGYAEP--TWEPLDNLADTAALDRFE 49
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 14-58 1.10e-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: 54.02  E-value: 1.10e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 604824794  14 ENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDV-RLLEAFE 58
Cdd:cd18974    4 EEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENApKAIQSYE 49
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 14-59 2.59e-09

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


Pssm-ID: 349321  Cd Length: 53  Bit Score: 53.25  E-value: 2.59e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794  14 ENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDV----RLLEAFES 59
Cdd:cd18965    4 EALLKKRQFNRKLEYLVKWHGLPESENTWEREKDIKHVshwkQLLKDLRA 53
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 10-58 3.99e-09

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: 52.56  E-value: 3.99e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794  10 VFAAENIQKKRI-RKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFE 58
Cdd:cd18960    1 VFVVERILDKRLgRNGGEEFLIKWQGFPESDSSWEPRENLQCDEMLEEFE 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 106-469 4.54e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  106 ATPHGNSSSTETNSAMSPPHSPPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPQPAEAKEPAAKP 185
Cdd:PHA03247 2591 APPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL 2670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  186 KPAGQSSSPPKGPPSSKshkeqdekSRPVIAAtgVEVSTGPAPPEKDPEP---VTAPVLKPNQAADVSPSCSPPVLESSK 262
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRA--------ARPTVGS--LTSLADPPPPPPTPEPaphALVSATPLPPGPAAARQASPALPAAPA 2740

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  263 KPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPpskmPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGS 342
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP----RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  343 A---PVARAPFARPPVTFKPISPRLAVSVSQQPHAVHHSHPPASHLavppvaARLGTGQLGPATVARISRPPthlvTSAV 419
Cdd:PHA03247 2817 AlppAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV------RRRPPSRSPAAKPAAPARPP----VRRL 2886

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 604824794  420 PSNATSAPSSQVVANSAGPNPSPTVATIVPVNTPAPPNPAHATTGQAPPQ 469
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
PHA03247 PHA03247
large tegument protein UL36; Provisional
 86-469 7.70e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.18  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794   86 DFRQDSNKAKSEDDTSNDAPATPHGNSSSTETNSAMSPPHSPPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQ 165
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  166 APTATPKPQPAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAAtgvevSTGPAPPEKDPEPVTAPVLKPNQ 245
Cdd:PHA03247 2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA-----PAPPAVPAGPATPGGPARPARPP 2761

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  246 AADVSPSCSPPVLESSKKPDTTGSAATKRKFEARP-LHMTSSPQQIPVP-----PAMQMHQPPPSKMPRLTRPADVPPVA 319
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESREsLPSPWDPADPPAAvlapaAALPPAASPAGPLPPPTSAQPTAPPP 2841

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  320 ATVPRPPPVVAATSTAPhfmngSAPVARAPFARPPVTfKPISPRlavsvsqqphavhhsHPPASHLAVPPVAARLGTGQL 399
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAP-----GGDVRRRPPSRSPAA-KPAAPA---------------RPPVRRLARPAVSRSTESFAL 2900

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  400 GPATVARISRPPThlvtsavPSNATSAPSSQvvansagPNPSPTVATIVPVNTPAPPNPAHATTGQAPPQ 469
Cdd:PHA03247 2901 PPDQPERPPQPQA-------PPPPQPQPQPP-------PPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 18-58 1.40e-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: 349320  Cd Length: 54  Bit Score: 51.18  E-value: 1.40e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 604824794  18 KKRIRKGRVEYLVKWRGWSHKYNTWEPEENILD-VRLLEAFE 58
Cdd:cd18964   12 SARDGPGKFLWLVKWDGYPIEDATWEPPENLGEhAKLIEDFE 53
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 11-58 1.92e-08

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: 50.64  E-value: 1.92e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILD--VRLLEAFE 58
Cdd:cd18976    1 YIVESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRrcAELVAAYD 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 123-472 3.01e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  123 PPHSPPPTLSPA----PAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPQPAEAKEPAAKPKPAGQSSSPPKGP 198
Cdd:PHA03247 2707 TPEPAPHALVSAtplpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP 2786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  199 PSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSPSCSPPVLESSKKPD------------- 265
Cdd:PHA03247 2787 AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrrp 2866

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  266 TTGSAATK---------RKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPP---VVAATS 333
Cdd:PHA03247 2867 PSRSPAAKpaaparppvRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrpqPPLAPT 2946

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  334 TAPHFMNGSAPVARAPFARPPVTFKPISPRLAVSVSQQP-HAVHHSHPPASHLAVPPVAARLGTGQL------GPATVAR 406
Cdd:PHA03247 2947 TDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSrEAPASSTPPLTGHSLSRVSSWASSLALheetdpPPVSLKQ 3026

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604824794  407 ISRPPTHLVTSAVPSNATSAPSSqvvANSAGPNPSPTVATIVPVNTPAPPNPAhATTGQAPPQHNG 472
Cdd:PHA03247 3027 TLWPPDDTEDSDADSLFDSDSER---SDLEALDPLPPEPHDPFAHEPDPATPE-AGARESPSSQFG 3088
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
 11-59 3.92e-08

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: 49.94  E-value: 3.92e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDV-RLLEAFES 59
Cdd:cd18973    1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAqKLLKKYYQ 50
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 10-59 4.84e-08

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: 49.44  E-value: 4.84e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794  10 VFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILD-VRLLEAFES 59
Cdd:cd18630    1 EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNcMKLVADYEA 51
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 11-59 1.18e-07

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


Pssm-ID: 349289  Cd Length: 49  Bit Score: 48.28  E-value: 1.18e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFES 59
Cdd:cd18639    1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRLLKQFHK 49
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
 27-52 1.36e-07

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. 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: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 48.90  E-value: 1.36e-07
                         10        20
                 ....*....|....*....|....*.
gi 604824794  27 EYLVKWRGWSHKYNTWEPEENILDVR 52
Cdd:cd18660   35 EFLVKWKGKSYLHCTWVTEETLEQLR 60
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
 23-50 2.45e-07

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. 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: 349313  Cd Length: 85  Bit Score: 48.44  E-value: 2.45e-07
                         10        20
                 ....*....|....*....|....*...
gi 604824794  23 KGRVEYLVKWRGWSHKYNTWEPEENILD 50
Cdd:cd18666   44 ETEIQYLIKWKGWSHIHNTWESEESLKD 71
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 11-58 2.47e-07

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: 47.67  E-value: 2.47e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794  11 FAAENIQKKRI--RKGRVEYLVKWRGWSHKYNTWEPEENILDVR-LLEAFE 58
Cdd:cd18640    1 EPVEKIVAKRFnpRKKTWEYLVKWENRSHHENTWEPMANLERCKyLLQMFE 51
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 11-58 4.21e-07

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


Pssm-ID: 349322  Cd Length: 49  Bit Score: 46.89  E-value: 4.21e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFE 58
Cdd:cd18966    1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGDEELLKEWE 48
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 16-49 4.73e-07

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: 46.67  E-value: 4.73e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 604824794  16 IQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENIL 49
Cdd:cd18634    8 VDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLL 41
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 8-58 7.59e-07

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: 46.16  E-value: 7.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAFE 58
Cdd:cd18978    1 DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVTQEDFNDKDMIDEYE 51
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 10-48 3.04e-06

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: 44.75  E-value: 3.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 604824794  10 VFAAENIQKKRIRK-GRVEYLVKWRGWSHKYNTWEPEENI 48
Cdd:cd18636    1 VYEVEDILADRVNKnGINEYYIKWAGYDWYDNTWEPEQNL 40
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 10-55 3.60e-06

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: 44.20  E-value: 3.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 604824794  10 VFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVR--LLE 55
Cdd:cd18633    1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKevLLE 48
PHA03247 PHA03247
large tegument protein UL36; Provisional
 232-555 3.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  232 DPEPVTAPVLKPnQAADVSPSCSPPVlesskkPDTTGSAATKRkfEARPlhmtsspqQIPVPPAMQMHQPPPSKMPRLTR 311
Cdd:PHA03247 2550 DPPPPLPPAAPP-AAPDRSVPPPRPA------PRPSEPAVTSR--ARRP--------DAPPQSARPRAPVDDRGDPRGPA 2612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  312 PADVPPVAATVPRPPPvvAATSTAPHFMNGSAPVARAPFARPPVTFKPISPRLAVSVSQQPHAVHHSHPPA--SHLAVPP 389
Cdd:PHA03247 2613 PPSPLPPDTHAPDPPP--PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrpRRRAARP 2690

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  390 VAARLgTGQLGPATVARISRPPTHLVTSAVPSN-ATSAPSSQVVANSAGPNPSPTVATIVPVNTPAPPnPAHATTGQAPP 468
Cdd:PHA03247 2691 TVGSL-TSLADPPPPPPTPEPAPHALVSATPLPpGPAAARQASPALPAAPAPPAVPAGPATPGGPARP-ARPPTTAGPPA 2768

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  469 QHNGPPPTATPVVPNGRESAAPHHGGGNDRENVCKPAVSAVSQGKPLHSHNGQAASPPTLLPPKEANAEPATAEPEYSPM 548
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848


                  ....*..
gi 604824794  549 AIIPDFW 555
Cdd:PHA03247 2849 SLPLGGS 2855
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
 9-52 4.00e-06

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. 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: 349312  Cd Length: 65  Bit Score: 44.68  E-value: 4.00e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 604824794   9 RVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVR 52
Cdd:cd18665   12 RLKEGLEEGELDDPKENYEFLIKWTDESHLHNTWETYESLKQVR 55
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 180-420 5.76e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.70  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  180 EPAAKPKPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPEPVTapvlkPNQAADVSPSCSPPVLE 259
Cdd:PRK10263  370 EPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQ-----PAQQPYYAPAPEQPVAG 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  260 SSKKPDTTGSAatkrkFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPadVPPVAATVPRPPPVVAATSTAPHFM 339
Cdd:PRK10263  445 NAWQAEEQQST-----FAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEP--EPVVEETKPARPPLYYFEEVEEKRA 517

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  340 NGSAPVAR--APFARPPVTFKPISPrlavsvSQQPHAVHHSHPPASHLAVPPVAARLGTGQLGPATVARISRPPTHLVTS 417
Cdd:PRK10263  518 REREQLAAwyQPIPEPVKEPEPIKS------SLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANS 591


                  ...
gi 604824794  418 AVP 420
Cdd:PRK10263  592 GGP 594
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 268-402 1.61e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.79  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 268 GSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVAR 347
Cdd:PRK14951 368 AAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL 447

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 604824794 348 APFARPPVTFKPISPrlAVSVSQQPHAVHHSHPPASHlavpPVAARLGTGQLGPA 402
Cdd:PRK14951 448 APAPPAQAAPETVAI--PVRVAPEPAVASAAPAPAAA----PAAARLTPTEEGDV 496
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
 16-50 2.08e-05

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. 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: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 42.25  E-value: 2.08e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 604824794  16 IQKKRIRKGRVEYLVKWRGWSHKYNTWEPEE-NILD 50
Cdd:cd18662   10 INHRVDKDGNTWYLVKWRDLPYDQSTWESEDdDIPD 45
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 8-57 2.36e-05

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: 42.17  E-value: 2.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794   8 ERVFAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILDVRLLEAF 57
Cdd:cd18962    1 EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDLNDKEILRKY 50
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
216-468 3.53e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.77  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 216 AATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSPSCSPPVLESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPA 295
Cdd:PRK07003 385 ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCD 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 296 MQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVArapfarppvtfkpisprlavsvSQQPHAV 375
Cdd:PRK07003 465 ERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAA----------------------ASREDAP 522

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 376 HHSHPPASHLAVP-PVAARLGTGQLGPATVARISRPPTHLVTSAVPSNATSAPSSQVVANSAGPNPSPTVATIVP----- 449
Cdd:PRK07003 523 AAAAPPAPEARPPtPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPtprar 602

                        250       260
                 ....*....|....*....|....*
gi 604824794 450 ------VNTPAPPNPAHATTGQAPP 468
Cdd:PRK07003 603 aatgdaPPNGAARAEQAAESRGAPP 627
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
 8-50 4.92e-05

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. 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: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 41.02  E-value: 4.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 604824794   8 ERVfaaenIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEENILD 50
Cdd:cd18659    6 ERI-----IAHREDDEGVTEYLVKWKGLPYDECTWESEEDISD 43
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
263-472 5.33e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 263 KPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGS 342
Cdd:PRK12323 364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 343 APVARAPFARPPVTFKPiSPRLAVSVSQQPHAVHHSHPPASHLAVPPVAARLGT-------GQLGPATVARISRPPTHLV 415
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAA-AARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPppweelpPEFASPAPAQPDAAPAGWV 522

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 604824794 416 TSAVPSNATSAPSSQVVANSAGPNPSPTVATIVPVNTPAPPNPAHATTGQAPPQHNG 472
Cdd:PRK12323 523 AESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
243-349 8.47e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.54  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 243 PNQAADVSPSCSPpvlESSKKPDTTGSAA--------------TKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSK-MP 307
Cdd:PRK14971 363 TQKGDDASGGRGP---KQHIKPVFTQPAAapqpsaaaaaspspSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPvNP 439

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 604824794 308 RLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVARAP 349
Cdd:PRK14971 440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQA 481
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 16-50 1.03e-04

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: 40.18  E-value: 1.03e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 604824794  16 IQKKRIRKGRVE-YLVKWRGWSHKYNTWEPEENILD 50
Cdd:cd18632    8 VDEKTDRNTAEPlYLVRWKNYSKNHDTWEPAENLSG 43
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 11-46 2.18e-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: 39.03  E-value: 2.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 604824794  11 FAAENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEE 46
Cdd:cd18972    1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKE 36
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
173-354 2.59e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 173 PQPAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKEQ---DEKSRPVIAATGVEVSTGPAPPEKDPEPVTAPVLKP-NQAAD 248
Cdd:PRK12323 385 PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVaaaPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaAAARP 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 249 VSPSCSPPVLESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQ-PPPSKMPRLTRPADVPPVAATVPRPPP 327
Cdd:PRK12323 465 AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAaPAGWVAESIPDPATADPDDAFETLAPA 544

                        170       180
                 ....*....|....*....|....*..
gi 604824794 328 VVAATSTAPhfmngSAPVARAPFARPP 354
Cdd:PRK12323 545 PAAAPAPRA-----AAATEPVVAPRPP 566
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
286-490 3.41e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 286 SPQQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVAR-APFARPPVTFKPISPRL 364
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARqASARGPGGAPAPAPAPA 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 365 AVSVSQQPHAVHHSHPPASHLAVPPVAArlgtGQLGPATVARISRPPTHLVTSAVPSNATSAPSSQVVANSAGPNPSPTV 444
Cdd:PRK12323 456 AAPAAAARPAAAGPRPVAAAAAAAPARA----APAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPAT 531

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 604824794 445 ATIVPVNTPAPPNPAHATtgqAPPQHNGPPPTATPVVPNGRESAAP 490
Cdd:PRK12323 532 ADPDDAFETLAPAPAAAP---APRAAAATEPVVAPRPPRASASGLP 574
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 242-436 4.85e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.93  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 242 KPNQAADVSPSCSPPVLESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPadvPPVAAT 321
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRA---QGATKA 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 322 VPRPPPVVAATSTAPHFMNGSAPVARAPFARPPVTFKPISPRLAVSVSQQPHAVHHSHPPAS-----HLAVPPVAARLGT 396
Cdd:PRK07994 439 KKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALkkaleHEKTPELAAKLAA 518

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 604824794 397 GQLGPATVARIsrppthlvtsaVPSNATSAPSSQVVANSA 436
Cdd:PRK07994 519 EAIERDPWAAL-----------VSQLGLPGLVEQLALNAW 547
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
127-392 6.02e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 127 PPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPqPAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKE 206
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAA-GAALAPKAAAAAAATRAEAPPAAPAPPATADR 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 207 QDE---KSRPVIAATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSPscsPPVLESSKKPDTTGSAATKRKFEARPLHM 283
Cdd:PRK07003 439 GDDaadGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPP---DAAFEPAPRAAAPSAATPAAVPDARAPAA 515

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 284 TSSPQQIPVPPAMQMHQPPPSkmPRLTRPADVPPVAAT---VPRPPPVVAATSTAphfmnGSAPVARAPFARPPVTFKPI 360
Cdd:PRK07003 516 ASREDAPAAAAPPAPEARPPT--PAAAAPAARAGGAAAaldVLRNAGMRVSSDRG-----ARAAAAAKPAAAPAAAPKPA 588

                        250       260       270
                 ....*....|....*....|....*....|..
gi 604824794 361 SPRLAVSVSQQPHAVHHSHPPASHLAVPPVAA 392
Cdd:PRK07003 589 APRVAVQVPTPRARAATGDAPPNGAARAEQAA 620
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 230-423 8.90e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.41  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 230 EKDPEPVTAPVLKPNQAADVSPSCSPPVLESSKKPDTTGSAATKRKFEARPlHMTSSPQQIPVP-PAMQMHQ-----PPP 303
Cdd:PHA03269  20 ANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDL-AQAPTPAASEKFdPAPAPHQaasraPDP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 304 SKMPRL----TRPADVPPVAATVPRPPPVVAATSTaphFMNGSAPVARAPFARPPVTFKPISPRLAVSVsqqphaVHHSH 379
Cdd:PHA03269  99 AVAPQLaaapKPDAAEAFTSAAQAHEAPADAGTSA---ASKKPDPAAHTQHSPPPFAYTRSMEHIACTH------GGIQF 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 604824794 380 PPASHLAVPPVAARLGTGQlgPATVARISRPPTHLVTSAVPSNA 423
Cdd:PHA03269 170 IPYFHKFILPCYLQIFTGQ--GAAFKQHELPKTYEEDFLDPEGA 211
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 214-305 2.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 214 VIAATGVEVSTGPAPPEKDP-EPVTAPVLKPNQAADVSPSCSPPVLESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPV 292
Cdd:PRK14950 359 LLVPVPAPQPAKPTAAAPSPvRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPV 438

                         90
                 ....*....|...
gi 604824794 293 PPAMQMHQPPPSK 305
Cdd:PRK14950 439 DEKPKYTPPAPPK 451
PHA03379 PHA03379
EBNA-3A; Provisional
 105-392 2.51e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.81  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 105 PATPHGNSSSTETNSAMSPPHSPPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPQPAEAkepaak 184
Cdd:PHA03379 425 PEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDGRPACAPV------ 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 185 PKPAGQSSsppkgppsskshkeqdeksRPVIAATGVEVSTGPAPPEKDPEPVtAPVLKPNQAADVSPSCSPPVLESSKKP 264
Cdd:PHA03379 499 PAPAGPIV-------------------RPWEASLSQVPGVAFAPVMPQPMPV-EPVPVPTVALERPVCPAPPLIAMQGPG 558

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 265 DTTGSAATKRKFEARPLHMT--SSPQQIPVP--PAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHF-M 339
Cdd:PHA03379 559 ETSGIVRVRERWRPAPWTPNppRSPSQMSVRdrLARLRAEAQPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSpF 638

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 604824794 340 NGSAPVARA---PFARPPVTFKPIsprlavsvsQQPHAVHHSHPP--ASHLAVPPVAA 392
Cdd:PHA03379 639 SQVADVMRAggvPAMQPQYFDLPL---------QQPISQGAPLAPlrASMGPVPPVPA 687
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
301-490 3.77e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 301 PPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVARAPFARPPVtfkpiSPRLAVSVSQQPHAVHHSHP 380
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA-----PEALAAARQASARGPGGAPA 449

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 381 PASHLAVPPVAArlgtgqlgPATVARISRPPThlvTSAVPSNATSAPSSQVVANSAGPNPSPTVATIVPVNTPAPPNPAH 460
Cdd:PRK12323 450 PAPAPAAAPAAA--------ARPAAAGPRPVA---AAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAP 518

                        170       180       190
                 ....*....|....*....|....*....|
gi 604824794 461 ATTGQAPPQHNGPPPTATPVVPNGRESAAP 490
Cdd:PRK12323 519 AGWVAESIPDPATADPDDAFETLAPAPAAA 548
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
325-553 4.83e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 325 PPPVVAATSTAPhfmngsAPVARAP-FARPPVTFKPISPRLAVSVSQQPHAVHHSHPPASHLAVPPVAARLGTGQLGPAT 403
Cdd:PRK12323 374 PATAAAAPVAQP------APAAAAPaAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 404 VARISRPPthlvtsAVPSNATSAPSsqvvansAGPNPSPTVATIVPVntPAPPNPAHATTGQAPPQHNGPPPTATPVVPN 483
Cdd:PRK12323 448 PAPAPAPA------AAPAAAARPAA-------AGPRPVAAAAAAAPA--RAAPAAAPAPADDDPPPWEELPPEFASPAPA 512

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 484 GRESAAPhhggGNDRENVCKPAVSAVSqgkplhshngqAASPPTLLPPKEANAEPATAEPEYSPMAIIPD 553
Cdd:PRK12323 513 QPDAAPA----GWVAESIPDPATADPD-----------DAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 17-47 4.93e-03

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: 35.75  E-value: 4.93e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 604824794  17 QKKRIRKGRVEYLVKWRGWSHKYNTWEPEEN 47
Cdd:cd18635   14 DPKKTGERGLYFKVRWKGYGPEEDTWEPIEG 44
CD_eEF3 cd18626
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ...
 14-46 5.09e-03

chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic elongation factor eEF3 (also known as EF-3, YEF3, and TEF3), a member of the ATP-binding cassette (ABC) family of proteins, is a ribosomal binding ATPase essential for fungal translation machinery. Until recently it was considered fungal-specific and therefore an attractive target for antifungal therapy; however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes, and translation elongation factor 3 activity has been demonstrated from a non-fungal species, Phytophthora infestans. 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. Chromodomain mutations in the ABC2 domain of eEF3 have been shown to reduce ATPase activity, but not ribosome binding. Thus, the chromodomain-like insertion is critical to eEF3 function. In addition to its elongation function, eEF3 has been shown to interact with mRNA in a translation independent manner, suggesting an additional, non-elongation function for this factor.


Pssm-ID: 349276 [Multi-domain]  Cd Length: 56  Bit Score: 35.65  E-value: 5.09e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 604824794  14 ENIQKKRIRKGRVEYLVKWRGWSHKYNTWEPEE 46
Cdd:cd18626    5 EKIVGRRKLKKSYEYEVKWKGMSSKDNSWIPRE 37
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
106-354 5.12e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 106 ATPHGNSSSTETNSAMSPPHSPPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPQPAEAKEPAAKP 185
Cdd:PRK07003 379 AVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARAS 458

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 186 KPAGQSSSPPKGPPSSKSHKEQDEKSRPVI----AATGVEVSTGPAPPEKDPEPVTAPVL--KPNQAADVSPSCSPPVLE 259
Cdd:PRK07003 459 ADSRCDERDAQPPADSGSASAPASDAPPDAafepAPRAAAPSAATPAAVPDARAPAAASRedAPAAAAPPAPEARPPTPA 538

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 260 SSKKP-DTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRltrpadVPPVAATVPRPPPVVAATSTAPHF 338
Cdd:PRK07003 539 AAAPAaRAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPA------APRVAVQVPTPRARAATGDAPPNG 612

                        250
                 ....*....|....*.
gi 604824794 339 MNGSAPVARAPFARPP 354
Cdd:PRK07003 613 AARAEQAAESRGAPPP 628
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 288-456 5.51e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 288 QQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAPhFMNGSAPVARAPFARPPVTfkpisprlavs 367
Cdd:PRK07994 363 APLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAP-AVPLPETTSQLLAARQQLQ----------- 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 368 vSQQPHAVHHSHPPASHLAVPPVAARLgtgqlgpATVARISRPPTHLVTSAVPSNATSAPSSQVVANSAGPNPSPTVATI 447
Cdd:PRK07994 431 -RAQGATKAKKSEPAAASRARPVNSAL-------ERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKK 502


                 ....*....
gi 604824794 448 VPVNTPAPP 456
Cdd:PRK07994 503 ALEHEKTPE 511
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 172-355 6.02e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 172 KPQPAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSP 251
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 252 SCSPPVLESSKKPDTTGSAATKRKFEARPLHMTSSPQQIPVPPAMQMHQPPPSKMPRLTRPADVPPVAATVPRPPPVVAA 331
Cdd:PRK07764 694 AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773

                        170       180
                 ....*....|....*....|....
gi 604824794 332 TSTAPHfmngSAPVARAPFARPPV 355
Cdd:PRK07764 774 PPPSPP----SEEEEMAEDDAPSM 793
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
319-549 6.67e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 319 AATVPRPPPVVAATSTAPHFMNGSAPVARAPFARPPVTFKPISPRLAVSVSQQPHAVhhSHPPASHLAVPPVAARLGTGQ 398
Cdd:PRK07003 366 GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATR--AEAPPAAPAPPATADRGDDAA 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 399 LGPATVARISRPPTHLVTSAVPSNATSAPSSQVVANSAGP-------NPSPTVATIVPVNTPAPPNPAHATTGQAP--PQ 469
Cdd:PRK07003 444 DGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDappdaafEPAPRAAAPSAATPAAVPDARAPAAASREdaPA 523

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 470 HNGPPPTATPVVPNGRESAAPHHGGGNDRENVCKPAVSAVSQGKPLHShnGQAASPPTLLPPKEANAEPATAEPEYSPMA 549
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARA--AAAAKPAAAPAAAPKPAAPRVAVQVPTPRA 601
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 216-336 6.69e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 6.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 216 AATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSPSCSPPVLESSKKPDTTGSAATkrkfEARPLHMTSSPQQIPVPPA 295
Cdd:PRK14951 378 KKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAP----AAAPAAAPAAVALAPAPPA 453

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 604824794 296 MQmhQPPPSKMPRLTRPADVPPVAATVPRPPPVVAATSTAP 336
Cdd:PRK14951 454 QA--APETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-555 7.19e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 39.51  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  175 PAEAKEPAAKPKPAGQSSSPPKGPPSSKSHKEQDEKSRPVIAATGVEVSTgPAPPEKDPEP-VTAPVlkPNQAADVSPSC 253
Cdd:pfam05109 466 PTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTT-PTPNATSPTPaVTTPT--PNATSPTLGKT 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  254 SPPVLESSKKPDTTGsaatkrkfearPLHMTSSPQQIPVPPAMQmHQPPPSKMPRLTRPADVPPVAATVPRpppvvaaTS 333
Cdd:pfam05109 543 SPTSAVTTPTPNATS-----------PTPAVTTPTPNATIPTLG-KTSPTSAVTTPTPNATSPTVGETSPQ-------AN 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  334 TAPHFMNG--SAPVARAP--FARPPVTF--KPISPRLAVSVSQQPHAVHHSHPPA------SHLAVPPVAARLGTGQLGP 401
Cdd:pfam05109 604 TTNHTLGGtsSTPVVTSPpkNATSAVTTgqHNITSSSTSSMSLRPSSISETLSPStsdnstSHMPLLTSAHPTGGENITQ 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  402 ATVARISrppTHLVTSAVPsnatsAPSSQVVANSAGPNPSPTVATIVPVNTPAPPNPAHATTGQAPPQHNGPPPTATPVV 481
Cdd:pfam05109 684 VTPASTS---THHVSTSSP-----APRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTG 755

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794  482 PNGRESAAPHHGGGNDRENVCKPAVS-AVSQGKPLHSHNGQAASPP----------TLLPPKEANAE-----PATAEPEY 545
Cdd:pfam05109 756 GKANSTTGGKHTTGHGARTSTEPTTDyGGDSTTPRTRYNATTYLPPstssklrprwTFTSPPVTTAQatvpvPPTSQPRF 835

                         410
                  ....*....|
gi 604824794  546 SPMAIIPDFW 555
Cdd:pfam05109 836 SNLSMLVLQW 845
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 307-433 7.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.31  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 307 PRLTRPADVPPVAATVPRPPPVVAATSTAPHFMNGSAPVARAPFARPPVTfKPISPRLAVSVSQQPHAVHHSHPPASHLA 386
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPA-APPAAAPPAPVAAPAAAAPAAAPAAAPAA 444

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 604824794 387 VPPVAARLGTGQLGPATVARISRPPTHLVTSAVPSNATSAPSSQVVA 433
Cdd:PRK14951 445 VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPT 491
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
421-547 7.41e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 7.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 421 SNATSAPSSQVVANSAGPNPS---PTVATIVPVNTPAPPNPAHATTGQAPPQHNGPPPTATPVVPNGRESAAPHHGGGND 497
Cdd:PRK12323 368 SGGGAGPATAAAAPVAQPAPAaaaPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 604824794 498 RENVCKPAVSAVSQGKPLHSHNGQAASPPTLLPPKEANAEPATAEPEYSP 547
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP 497
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
103-323 8.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.09  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 103 DAPATPHGNSSSTETNSAMSPPHSPPPTLSPAPAEDKESSAVSAVSRLSASPSASSQQQTAQQAPTATPKPQPAEAKEPA 182
Cdd:PRK12323 382 VAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAA 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 183 AKPKPAGQSSSPPKGPPSSkshkeqdekSRPVIAATGVEVSTGPAPPEKDPEPVTAPVLKPNQAADVSPSCSPPVLESSK 262
Cdd:PRK12323 462 ARPAAAGPRPVAAAAAAAP---------ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 604824794 263 KPDTTGSAATKRKFEA--RPLHMTSSPQQIPVPPAMQMHQPPPskmprlTRPADVPPVAATVP 323
Cdd:PRK12323 533 DPDDAFETLAPAPAAApaPRAAAATEPVVAPRPPRASASGLPD------MFDGDWPALAARLP 589
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 293-436 8.96e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604824794 293 PPAMQMHQPPPSKMPrLTRPADVPPVAATVPRPPPVVAATSTAPHFMNG-SAPVARAPFAR--PPVTFKPISPRLAVSVS 369
Cdd:PRK14951 366 PAAAAEAAAPAEKKT-PARPEAAAPAAAPVAQAAAAPAPAAAPAAAASApAAPPAAAPPAPvaAPAAAAPAAAPAAAPAA 444

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604824794 370 QQPhAVHHSHPPASHLAVPPVAARLGTGQLGPAtVARISRPPTHLVTSAVPSNATSAPSSQVVANSA 436
Cdd:PRK14951 445 VAL-APAPPAQAAPETVAIPVRVAPEPAVASAA-PAPAAAPAAARLTPTEEGDVWHATVQQLAAAEA 509
 
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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