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Conserved domains on  [gi|2462515612|ref|XP_054195685|]
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chromodomain-helicase-DNA-binding protein 1-like isoform X2 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase; macro domain-containing protein( domain architecture ID 13327344)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA| macro domain-containing protein may bind compounds such as O-acetyl-ADP-ribose, mono- and poly-ADP-ribose, and catalyze reactions such as O-acetyl-ADP-ribose deacetylation and reversal of ADP-ribosylation of mono-ADP-ribosylated substrates; similar to viral non-structural protein 3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 289-439 6.29e-97

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


:

Pssm-ID: 394880  Cd Length: 152  Bit Score: 288.39  E-value: 6.29e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462515612 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-272 3.45e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 3.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462515612  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
 
Name Accession Description Interval E-value
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 289-439 6.29e-97

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 288.39  E-value: 6.29e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462515612 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-272 3.45e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 3.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462515612  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 2-43 3.38e-18

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 80.60  E-value: 3.38e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462515612   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 43
Cdd:cd18793    94 NLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 2-68 1.25e-16

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 82.58  E-value: 1.25e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462515612   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 68
Cdd:COG0553   616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
HELICc smart00490
helicase superfamily c-terminal domain;
1-32 1.85e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 45.67  E-value: 1.85e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462515612    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:smart00490  51 LDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1-32 2.21e-06

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 46.43  E-value: 2.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462515612   1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
 
Name Accession Description Interval E-value
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 289-439 6.29e-97

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 288.39  E-value: 6.29e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 289 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 367
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462515612 368 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 289-439 1.41e-26

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 104.26  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 289 SLKYVSGDVTHPQagaEDALIVHCVDDSGHWGRGGLFTALEK--RSAEPRKIYELAGkmkdlsLGGVLLFPVDDKesrnk 366
Cdd:cd02901     1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKKpgRVEELRAQCKKKL------LGGVAVLKRDGV----- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462515612 367 gQDLLALIVAQHRDRSNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 439
Cdd:cd02901    67 -KRYIYYLITKKSYGPK----PTYEALRSSLEELReHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-272 3.45e-21

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 97.18  E-value: 3.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPA 80
Cdd:PLN03142   554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKT 630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612   81 ADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGK 142
Cdd:PLN03142   631 VNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENK 709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612  143 NHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDR 216
Cdd:PLN03142   710 LDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYL 783

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462515612  217 QKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 272
Cdd:PLN03142   784 MQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 2-43 3.38e-18

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 80.60  E-value: 3.38e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462515612   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 43
Cdd:cd18793    94 NLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 2-68 1.25e-16

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 82.58  E-value: 1.25e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462515612   2 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 68
Cdd:COG0553   616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
HELICc smart00490
helicase superfamily c-terminal domain;
1-32 1.85e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 45.67  E-value: 1.85e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462515612    1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:smart00490  51 LDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1-32 2.21e-06

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 46.43  E-value: 2.21e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462515612   1 MNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 32
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 308-434 7.66e-05

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 42.00  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 308 LIVHCVDDSGHWGrGGLFTALEKRSAEPRKIYELAGKMKD-LSLGGVLLfpvddkesrNKGQDLLALIVAqHrdrSNVLS 386
Cdd:cd02749     2 AIVNPANNDLYLG-GGVAKAISKKAGGDLQEECEERKKNGyLKVGEVAV---------TKGGNLPARYII-H---VVGPV 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462515612 387 GIKMAALEEGLKKIF-----LAAKKKKASVHLPRIGHATKGFNWYGTERLIRK 434
Cdd:cd02749    68 ASSKKKTYEPLKKCVknclsLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLE 120
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 136-247 2.37e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 136 RDQEEGKNHmylfegKDYSKEPSKEDRKSFEQLvnlQKTLLEKASQEGRSlrnkgsvlipGLVEgsTKRKRVLSPEELED 215
Cdd:pfam17380 466 RQQEEERKR------KKLELEKEKRDRKRAEEQ---RRKILEKELEERKQ----------AMIE--EERKRKLLEKEMEE 524

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462515612 216 RQKKRQEaaAKRRRLIEEKKRQKEEAEHKKKM 247
Cdd:pfam17380 525 RQKAIYE--EERRREAEEERRKQQEMEERRRI 554
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
 219-268 4.60e-03

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


Pssm-ID: 462043 [Multi-domain]  Cd Length: 192  Bit Score: 38.28  E-value: 4.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462515612 219 KRQEA-AAKRRRLIE----------EKKRQKEEAEHKKKMAWWES----NNYQSFCLPSEESEPE 268
Cdd:pfam06936  80 KRQEAlEASRLRMQEeldaqaekfkEKQKQLEEEKRRQKIEMWESmqegKSYKGNAKLAQEETEE 144
Caldesmon pfam02029
Caldesmon;
155-245 8.25e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 38.70  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462515612 155 KEPSKEDRKSFEQ-LVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRK---RVLSPEEledrQKKRQEAAAKRRRL 230
Cdd:pfam02029 236 REEEAEVFLEAEQkLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREerrKLLEEEE----QRRKQEEAERKLRE 311

                          90
                  ....*....|....*
gi 2462515612 231 IEEKKRQKEEAEHKK 245
Cdd:pfam02029 312 EEEKRRMKEEIERRR 326
 
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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