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Conserved domains on  [gi|1720398297|ref|XP_030105473|]
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protein PAXX isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAXX super family cl21222
PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins ...
 10-165 1.07e-79

PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins that belong to the XRCC4 superfamily of DNA-double-strand break-repair proteins. PAXX interacts directly with DSB-repair protein Ku and is recruited to DNA-damage sites in cells thus functioning with XRCC4 and XLF to bring about DSB repair and cell survival in response to DSB-inducing agents.


The actual alignment was detected with superfamily member pfam15384:

Pssm-ID: 464691  Cd Length: 194  Bit Score: 236.59  E-value: 1.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297  10 LCILPPGSGSPRLVCYCERDSGGDGDRDdFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVTV 89
Cdd:pfam15384   1 LCTVPPGPGQPRYVCYCERKEGGAGDRV-FNLYVTDAAEVWSTEFTPDSLAQLKARFGLKSAEDYTLRFRAACEQGAVSL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398297  90 SLQEDRALITLSGDTPALAFDLSKVPSPEAAPRLQALTLSLAEHVCNLERRLaAAEETITSPKKNTQPAGTQFLPE 165
Cdd:pfam15384  80 TLQEDRASLTLGGGPEALSFDLSKVPSPEAAPELKALLFGMAERLCQLESRL-AAEESSFSPRKSYQPAGAQFLPD 154
 
Name Accession Description Interval E-value
PAXX pfam15384
PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins ...
 10-165 1.07e-79

PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins that belong to the XRCC4 superfamily of DNA-double-strand break-repair proteins. PAXX interacts directly with DSB-repair protein Ku and is recruited to DNA-damage sites in cells thus functioning with XRCC4 and XLF to bring about DSB repair and cell survival in response to DSB-inducing agents.


Pssm-ID: 464691  Cd Length: 194  Bit Score: 236.59  E-value: 1.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297  10 LCILPPGSGSPRLVCYCERDSGGDGDRDdFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVTV 89
Cdd:pfam15384   1 LCTVPPGPGQPRYVCYCERKEGGAGDRV-FNLYVTDAAEVWSTEFTPDSLAQLKARFGLKSAEDYTLRFRAACEQGAVSL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398297  90 SLQEDRALITLSGDTPALAFDLSKVPSPEAAPRLQALTLSLAEHVCNLERRLaAAEETITSPKKNTQPAGTQFLPE 165
Cdd:pfam15384  80 TLQEDRASLTLGGGPEALSFDLSKVPSPEAAPELKALLFGMAERLCQLESRL-AAEESSFSPRKSYQPAGAQFLPD 154
HD_PAXX_N cd22286
N-terminal head domain found in paralog of XRCC4 and XLF, and similar proteins; Paralog of ...
 9-114 8.39e-31

N-terminal head domain found in paralog of XRCC4 and XLF, and similar proteins; Paralog of XRCC4 and XLF (PAXX), also called XRCC4-like small protein, is a paralog of X-ray repair cross-complementing protein 4 (XRCC4) and XRCC4-like factor (XLF). It is involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks (DSBs) in DNA. It may act as a scaffold required to stabilize the DSB-repair protein Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites in cells. It functions with XRCC4 and XLF to bring about DSB repair and cell survival in response to DSB-inducing agents. Similar to XRCC4 and XLF, PAXX monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. This model corresponds to the N-terminal head domain of PAXX, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and CCDC61.


Pssm-ID: 409003  Cd Length: 102  Bit Score: 108.88  E-value: 8.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297   9 PLCILPPGSGSPRLVCYCERDSGGdgdrddFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVT 88
Cdd:cd22286     3 LLCTVTDGNDGSRYLCYTRLTNDS------FNICVTDGVDVWSTDFTEEELEEHRDLAGLSSTEDYLSKIRSAFESGTLS 76

                          90       100
                  ....*....|....*....|....*.
gi 1720398297  89 VSLQEDRALITLSGDTPALAFDLSKV 114
Cdd:cd22286    77 LTVQDSKATLTLGKGPSALTFDLYEL 102
 
Name Accession Description Interval E-value
PAXX pfam15384
PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins ...
 10-165 1.07e-79

PAXX, PAralog of XRCC4 and XLF, also called C9orf142; PAXX is a set of eukaryotic proteins that belong to the XRCC4 superfamily of DNA-double-strand break-repair proteins. PAXX interacts directly with DSB-repair protein Ku and is recruited to DNA-damage sites in cells thus functioning with XRCC4 and XLF to bring about DSB repair and cell survival in response to DSB-inducing agents.


Pssm-ID: 464691  Cd Length: 194  Bit Score: 236.59  E-value: 1.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297  10 LCILPPGSGSPRLVCYCERDSGGDGDRDdFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVTV 89
Cdd:pfam15384   1 LCTVPPGPGQPRYVCYCERKEGGAGDRV-FNLYVTDAAEVWSTEFTPDSLAQLKARFGLKSAEDYTLRFRAACEQGAVSL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398297  90 SLQEDRALITLSGDTPALAFDLSKVPSPEAAPRLQALTLSLAEHVCNLERRLaAAEETITSPKKNTQPAGTQFLPE 165
Cdd:pfam15384  80 TLQEDRASLTLGGGPEALSFDLSKVPSPEAAPELKALLFGMAERLCQLESRL-AAEESSFSPRKSYQPAGAQFLPD 154
HD_PAXX_N cd22286
N-terminal head domain found in paralog of XRCC4 and XLF, and similar proteins; Paralog of ...
 9-114 8.39e-31

N-terminal head domain found in paralog of XRCC4 and XLF, and similar proteins; Paralog of XRCC4 and XLF (PAXX), also called XRCC4-like small protein, is a paralog of X-ray repair cross-complementing protein 4 (XRCC4) and XRCC4-like factor (XLF). It is involved in non-homologous end joining (NHEJ), a major pathway to repair double-strand breaks (DSBs) in DNA. It may act as a scaffold required to stabilize the DSB-repair protein Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites in cells. It functions with XRCC4 and XLF to bring about DSB repair and cell survival in response to DSB-inducing agents. Similar to XRCC4 and XLF, PAXX monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. This model corresponds to the N-terminal head domain of PAXX, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and CCDC61.


Pssm-ID: 409003  Cd Length: 102  Bit Score: 108.88  E-value: 8.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297   9 PLCILPPGSGSPRLVCYCERDSGGdgdrddFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVT 88
Cdd:cd22286     3 LLCTVTDGNDGSRYLCYTRLTNDS------FNICVTDGVDVWSTDFTEEELEEHRDLAGLSSTEDYLSKIRSAFESGTLS 76

                          90       100
                  ....*....|....*....|....*.
gi 1720398297  89 VSLQEDRALITLSGDTPALAFDLSKV 114
Cdd:cd22286    77 LTVQDSKATLTLGKGPSALTFDLYEL 102
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 9-114 1.05e-17

N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.


Pssm-ID: 408999  Cd Length: 115  Bit Score: 75.66  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398297   9 PLCILPPGSGSPRLVCYCERDSGGDGDrddFNLYVTDAAELWSTCFSPDSLARLKARFG-LSGAEDIHSRFRAACQQ--- 84
Cdd:cd22210     1 PWRPLPLHVVLEELTFKVETEVANERG---LRLHVSDDAFLWTGEVSESDISQLKNDQGiLVDFASFPGKLRSALEKcil 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720398297  85 ----QAVTVSLQEDRALITL----SGDTPALAFDLSKV 114
Cdd:cd22210    78 asdrFTFVLTIRGDEAYLKLveilDEQLPHITFALRKV 115
 
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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