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Conserved domains on  [gi|297283363|ref|XP_001094220|]
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PREDICTED: structure-specific endonuclease subunit SLX4 [Macaca mulatta]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Slx4 pfam09494
Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found ...
1696-1755 4.11e-16

Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearing the 5' non-homologous arm at the branch junction and thus generating ligatable nicked products from 5'-flap or replication fork substrates.


:

Pssm-ID: 255396  Cd Length: 62  Bit Score: 76.06  E-value: 4.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297283363  1696 TDEALRCYIRSKPALYQKVLLYQPFELGELQAELKQNGLC--VSSRRLLDFLDTHCITFTTA 1755
Cdd:pfam09494    1 LFEALTEAIKSDPDLYEKILTYEPIELEELQAWLKAAGIDrrVDEDLLKEWLDSQGITFTTA 62
BTB super family cl02518
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
635-742 3.27e-07

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


The actual alignment was detected with superfamily member pfam00651:

Pssm-ID: 271586  Cd Length: 107  Bit Score: 50.74  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   635 FGAMVNNPHLSDVQFQTDsGEVLYAHKFVLYARCPLLiqyvnNEGFSAVEDGILTQRVLLGDVSTEAACAFLHYLYTaDT 714
Cdd:pfam00651    1 LNELRENGELCDVTLVVG-DKEFKAHKAVLAACSPYF-----KALFSSNEEESSVVEITLEDVSPEDFEALLEFIYT-GK 73
                           90       100
                   ....*....|....*....|....*...
gi 297283363   715 GLPPGLSSELSSLAHRFGVSELVHLCEQ 742
Cdd:pfam00651   74 LISEENVEDLLALADKLQIPALIDKCEE 101
 
Name Accession Description Interval E-value
Slx4 pfam09494
Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found ...
1696-1755 4.11e-16

Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearing the 5' non-homologous arm at the branch junction and thus generating ligatable nicked products from 5'-flap or replication fork substrates.


Pssm-ID: 255396  Cd Length: 62  Bit Score: 76.06  E-value: 4.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297283363  1696 TDEALRCYIRSKPALYQKVLLYQPFELGELQAELKQNGLC--VSSRRLLDFLDTHCITFTTA 1755
Cdd:pfam09494    1 LFEALTEAIKSDPDLYEKILTYEPIELEELQAWLKAAGIDrrVDEDLLKEWLDSQGITFTTA 62
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
635-742 3.27e-07

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 250031  Cd Length: 107  Bit Score: 50.74  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   635 FGAMVNNPHLSDVQFQTDsGEVLYAHKFVLYARCPLLiqyvnNEGFSAVEDGILTQRVLLGDVSTEAACAFLHYLYTaDT 714
Cdd:pfam00651    1 LNELRENGELCDVTLVVG-DKEFKAHKAVLAACSPYF-----KALFSSNEEESSVVEITLEDVSPEDFEALLEFIYT-GK 73
                           90       100
                   ....*....|....*....|....*...
gi 297283363   715 GLPPGLSSELSSLAHRFGVSELVHLCEQ 742
Cdd:pfam00651   74 LISEENVEDLLALADKLQIPALIDKCEE 101
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
653-742 1.31e-06

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585  Cd Length: 97  Bit Score: 48.84  E-value: 1.31e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363    653 SGEVLYAHKFVLYARCPLLIQYVNNEGFSAVEDGILtqrvlLGDVSTEAACAFLHYLYTADTGLPPGLSSELSSLAHRFG 732
Cdd:smart00225    7 GGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIY-----LDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQ 81
                            90
                    ....*....|
gi 297283363    733 VSELVHLCEQ 742
Cdd:smart00225   82 IPGLVELCEE 91
Daxx pfam03344
Daxx Family; The Daxx protein (also known as the Fas-binding protein) is thought to play a ...
753-1037 5.07e-04

Daxx Family; The Daxx protein (also known as the Fas-binding protein) is thought to play a role in apoptosis, but precise role played by Daxx remains to be determined. Daxx forms a complex with Axin.


Pssm-ID: 251886 [Multi-domain]  Cd Length: 715  Bit Score: 43.75  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   753 PWEEKEAENCESRAENFQELLRSMWADEEEEAEtllkskDHEEDQENVNEAEMEeiyefAATQRKLLQEEKAVGAGEDAD 832
Cdd:pfam03344  440 EEEESVEEEEEEEEEEEEEEQESEEEEGEDEEE------EEEVEADNGSEEEME-----GSSEGDGDGEEPEEDAERRNS 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   833 WLEGGSPVSGQllasvQVQEQSDKVEEMEPSEPGRDEATTTwEKVGQCPLPPpqgqrsgAWGAEAPEQEALGRSSCSTPS 912
Cdd:pfam03344  509 EMAGISRMSEG-----QQPRGSSVQPESPQEEPLQPESMDA-ESVGEESDEE-------LLAEESPLSSHTELEGVATPV 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   913 RGCRAERKEGPlPHSDGAGDYEQlfSSTQGEISELSRVTSEP----EERSGTVRERGLEVSHRLAPWQVspphpcrflLG 988
Cdd:pfam03344  576 ETKISSSRKLP-PPPVSTSLEND--SATVTSTTRNGNVSPHTpqdeQPPSGRKRKRKEEVESEPLGNQY---------LR 643
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 297283363   989 PPQGRSPRGshQPHRTSGLpLSTPRSRGGTSQVGSPT-------SLSPAVPSKQKR 1037
Cdd:pfam03344  644 HHNGSEKDG--LPAPMDPV-TSCSPVADSSTRVDTPShelvtssPQTPGDPPKKNK 696
PHA03247 PHA03247
large tegument protein UL36; Provisional
421-636 7.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363  421 PPVSPPLLLVQDSETTGRQIEDRVALLLSEEVELSSTPPLPASRILKEG----WERAGQCPPPPECKQSFLWEGSALTGA 496
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgslTSLADPPPPPPTPEPAPHALVSATPLP 2722
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363  497 WATEAFYTARLVPPLVPQRPAQglmqePVLPLVPPEHSERRSPALHGTPPAGCGSRGPSPSASQREQQALQDLVDLAREG 576
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAV-----PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297283363  577 LSASPWPSSGGLAGSEGAAGLDVVP---GGLPLTGFVVPSQDKHPERGGRTSLSLGLLVADFG 636
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860
 
Name Accession Description Interval E-value
Slx4 pfam09494
Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found ...
1696-1755 4.11e-16

Slx4 endonuclease; The Slx4 protein is a heteromeric structure-specific endonuclease found from fungi to mammals. Slx4 with Slx1 acts as a nuclease on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures by cleaving the strand bearing the 5' non-homologous arm at the branch junction and thus generating ligatable nicked products from 5'-flap or replication fork substrates.


Pssm-ID: 255396  Cd Length: 62  Bit Score: 76.06  E-value: 4.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297283363  1696 TDEALRCYIRSKPALYQKVLLYQPFELGELQAELKQNGLC--VSSRRLLDFLDTHCITFTTA 1755
Cdd:pfam09494    1 LFEALTEAIKSDPDLYEKILTYEPIELEELQAWLKAAGIDrrVDEDLLKEWLDSQGITFTTA 62
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
635-742 3.27e-07

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 250031  Cd Length: 107  Bit Score: 50.74  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   635 FGAMVNNPHLSDVQFQTDsGEVLYAHKFVLYARCPLLiqyvnNEGFSAVEDGILTQRVLLGDVSTEAACAFLHYLYTaDT 714
Cdd:pfam00651    1 LNELRENGELCDVTLVVG-DKEFKAHKAVLAACSPYF-----KALFSSNEEESSVVEITLEDVSPEDFEALLEFIYT-GK 73
                           90       100
                   ....*....|....*....|....*...
gi 297283363   715 GLPPGLSSELSSLAHRFGVSELVHLCEQ 742
Cdd:pfam00651   74 LISEENVEDLLALADKLQIPALIDKCEE 101
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
653-742 1.31e-06

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585  Cd Length: 97  Bit Score: 48.84  E-value: 1.31e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363    653 SGEVLYAHKFVLYARCPLLIQYVNNEGFSAVEDGILtqrvlLGDVSTEAACAFLHYLYTADTGLPPGLSSELSSLAHRFG 732
Cdd:smart00225    7 GGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIY-----LDDVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQ 81
                            90
                    ....*....|
gi 297283363    733 VSELVHLCEQ 742
Cdd:smart00225   82 IPGLVELCEE 91
Daxx pfam03344
Daxx Family; The Daxx protein (also known as the Fas-binding protein) is thought to play a ...
753-1037 5.07e-04

Daxx Family; The Daxx protein (also known as the Fas-binding protein) is thought to play a role in apoptosis, but precise role played by Daxx remains to be determined. Daxx forms a complex with Axin.


Pssm-ID: 251886 [Multi-domain]  Cd Length: 715  Bit Score: 43.75  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   753 PWEEKEAENCESRAENFQELLRSMWADEEEEAEtllkskDHEEDQENVNEAEMEeiyefAATQRKLLQEEKAVGAGEDAD 832
Cdd:pfam03344  440 EEEESVEEEEEEEEEEEEEEQESEEEEGEDEEE------EEEVEADNGSEEEME-----GSSEGDGDGEEPEEDAERRNS 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   833 WLEGGSPVSGQllasvQVQEQSDKVEEMEPSEPGRDEATTTwEKVGQCPLPPpqgqrsgAWGAEAPEQEALGRSSCSTPS 912
Cdd:pfam03344  509 EMAGISRMSEG-----QQPRGSSVQPESPQEEPLQPESMDA-ESVGEESDEE-------LLAEESPLSSHTELEGVATPV 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363   913 RGCRAERKEGPlPHSDGAGDYEQlfSSTQGEISELSRVTSEP----EERSGTVRERGLEVSHRLAPWQVspphpcrflLG 988
Cdd:pfam03344  576 ETKISSSRKLP-PPPVSTSLEND--SATVTSTTRNGNVSPHTpqdeQPPSGRKRKRKEEVESEPLGNQY---------LR 643
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 297283363   989 PPQGRSPRGshQPHRTSGLpLSTPRSRGGTSQVGSPT-------SLSPAVPSKQKR 1037
Cdd:pfam03344  644 HHNGSEKDG--LPAPMDPV-TSCSPVADSSTRVDTPShelvtssPQTPGDPPKKNK 696
PHA03247 PHA03247
large tegument protein UL36; Provisional
421-636 7.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363  421 PPVSPPLLLVQDSETTGRQIEDRVALLLSEEVELSSTPPLPASRILKEG----WERAGQCPPPPECKQSFLWEGSALTGA 496
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgslTSLADPPPPPPTPEPAPHALVSATPLP 2722
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297283363  497 WATEAFYTARLVPPLVPQRPAQglmqePVLPLVPPEHSERRSPALHGTPPAGCGSRGPSPSASQREQQALQDLVDLAREG 576
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAV-----PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297283363  577 LSASPWPSSGGLAGSEGAAGLDVVP---GGLPLTGFVVPSQDKHPERGGRTSLSLGLLVADFG 636
Cdd:PHA03247 2798 LPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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