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Conserved domains on  [gi|2217325897|ref|XP_047299442|]
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septin-10 isoform X8 [Homo sapiens]

Protein Classification

septin family protein( domain architecture ID 10110922)

septin family protein, a filament-forming cytoskeletal GTPase, is involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924|GO:0061640|GO:0060090
PubMed:  14611653|12445407|12111093|18478031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 94-293 2.53e-106

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


:

Pssm-ID: 206649  Cd Length: 275  Bit Score: 314.87  E-value: 2.53e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897  94 DQMMNRY-YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKA 172
Cdd:cd01850    74 DNINNSDcWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 173 DTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVE 250
Cdd:cd01850   153 DTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVE 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217325897 251 NENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 293
Cdd:cd01850   233 NEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 231-365 4.30e-03

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 231 KVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRhyelyRRCKL----EEMGFTDVGPENKPVSV 306
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217325897 307 QETYEAKRHEFHGERQRK--EEEMKQMfvQRVKEKEAILKEAEREL--QAKFEHLKRLHQEER 365
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEER--QKAIYEEERRREAEEERrkQQEMEERRRIQEQMR 559
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 94-293 2.53e-106

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 314.87  E-value: 2.53e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897  94 DQMMNRY-YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKA 172
Cdd:cd01850    74 DNINNSDcWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 173 DTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVE 250
Cdd:cd01850   153 DTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVE 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217325897 251 NENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 293
Cdd:cd01850   233 NEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 94-291 2.86e-83

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 256.07  E-value: 2.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897  94 DQMMNRY-YQPIVDYIDAQFEAYLQEELKIKRSLFTyhDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKA 172
Cdd:pfam00735  73 DAIDNSNcWRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 173 DTVSKTELQKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQV 249
Cdd:pfam00735 151 DTLTPDELQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEV 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217325897 250 ENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 291
Cdd:pfam00735 231 ENPSHCDFLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 102-359 3.88e-82

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 256.48  E-value: 3.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 102 QPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQ 181
Cdd:COG5019   103 EPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 182 KFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 258
Cdd:COG5019   182 EFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 259 KLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEFHGERQRKEE-EMKQMFVQRVK 337
Cdd:COG5019   262 KLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEIHEARLNEEErELKKKFTEKIR 327

                         250       260
                  ....*....|....*....|..
gi 2217325897 338 EKEAILKEAERELQAKFEHLKR 359
Cdd:COG5019   328 EKEKRLEELEQNLIEERKELNS 349
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 231-365 4.30e-03

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: 39.34  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 231 KVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRhyelyRRCKL----EEMGFTDVGPENKPVSV 306
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217325897 307 QETYEAKRHEFHGERQRK--EEEMKQMfvQRVKEKEAILKEAEREL--QAKFEHLKRLHQEER 365
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEER--QKAIYEEERRREAEEERrkQQEMEERRRIQEQMR 559
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 302-353 6.15e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 34.94  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217325897 302 KPVSVQETYEAKRHEFHGERQ---RKEEEMKQMFVQRVKEKEAILKEAERELQAK 353
Cdd:cd22249     3 KPGEIREEYEAQLKKLEEERRkerEEEEKASEELIRKLQEEEERQRKREREEQLK 57
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 94-293 2.53e-106

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 314.87  E-value: 2.53e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897  94 DQMMNRY-YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKA 172
Cdd:cd01850    74 DNINNSDcWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 173 DTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVE 250
Cdd:cd01850   153 DTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVE 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217325897 251 NENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 293
Cdd:cd01850   233 NEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 94-291 2.86e-83

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 256.07  E-value: 2.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897  94 DQMMNRY-YQPIVDYIDAQFEAYLQEELKIKRSLFTyhDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKA 172
Cdd:pfam00735  73 DAIDNSNcWRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 173 DTVSKTELQKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQV 249
Cdd:pfam00735 151 DTLTPDELQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEV 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217325897 250 ENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 291
Cdd:pfam00735 231 ENPSHCDFLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 102-359 3.88e-82

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 256.48  E-value: 3.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 102 QPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQ 181
Cdd:COG5019   103 EPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 182 KFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 258
Cdd:COG5019   182 EFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 259 KLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEFHGERQRKEE-EMKQMFVQRVK 337
Cdd:COG5019   262 KLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEIHEARLNEEErELKKKFTEKIR 327

                         250       260
                  ....*....|....*....|..
gi 2217325897 338 EKEAILKEAERELQAKFEHLKR 359
Cdd:COG5019   328 EKEKRLEELEQNLIEERKELNS 349
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 231-365 4.30e-03

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: 39.34  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325897 231 KVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRhyelyRRCKL----EEMGFTDVGPENKPVSV 306
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217325897 307 QETYEAKRHEFHGERQRK--EEEMKQMfvQRVKEKEAILKEAEREL--QAKFEHLKRLHQEER 365
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEER--QKAIYEEERRREAEEERrkQQEMEERRRIQEQMR 559
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 302-353 6.15e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 34.94  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217325897 302 KPVSVQETYEAKRHEFHGERQ---RKEEEMKQMFVQRVKEKEAILKEAERELQAK 353
Cdd:cd22249     3 KPGEIREEYEAQLKKLEEERRkerEEEEKASEELIRKLQEEEERQRKREREEQLK 57
DUF349 pfam03993
Domain of Unknown Function (DUF349); This domain is found singly or as up to five tandem ...
 307-363 7.91e-03

Domain of Unknown Function (DUF349); This domain is found singly or as up to five tandem repeats in a small set of bacterial proteins. There are two or three alpha-helices, and possibly a beta-strand.


Pssm-ID: 427636 [Multi-domain]  Cd Length: 73  Bit Score: 34.84  E-value: 7.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217325897 307 QETYEAKRHEFHGERQRKEEEmkqmfvqRVKEKEAILKEAE------RELQAKFEHLKRLHQE 363
Cdd:pfam03993  10 CDAFFDRRKAFFEELDAEREE-------NLEKKEALIEEAEaladstTDWKAATKELRELQEE 65
 
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.
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