NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30519993|ref|NP_848758|]
View 

Fanconi anemia core complex-associated protein 24 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 17-139 5.83e-72

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


:

Pssm-ID: 410852  Cd Length: 123  Bit Score: 214.37  E-value: 5.83e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  17 GHIVASEKWRGSQLAQEMQGKVRLIFEEGLASADFYLSSKSCILYVTEADLVAGHGYRKRLARFRNSSHLQGIIIVEKTQ 96
Cdd:cd20076   1 GHILVNEKWRGSELVKSLQGKVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30519993  97 MSEQYFPAVQKFTVLDLGMVLLPVASQSEASCLIIHLVQEQTR 139
Cdd:cd20076  81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 166-218 7.26e-13

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


:

Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 61.39  E-value: 7.26e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30519993   166 IPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFTQPKRQQ 218
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPANRE 62
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 17-139 5.83e-72

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


Pssm-ID: 410852  Cd Length: 123  Bit Score: 214.37  E-value: 5.83e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  17 GHIVASEKWRGSQLAQEMQGKVRLIFEEGLASADFYLSSKSCILYVTEADLVAGHGYRKRLARFRNSSHLQGIIIVEKTQ 96
Cdd:cd20076   1 GHILVNEKWRGSELVKSLQGKVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30519993  97 MSEQYFPAVQKFTVLDLGMVLLPVASQSEASCLIIHLVQEQTR 139
Cdd:cd20076  81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 11-135 4.10e-63

FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the FANCM protein. This domain is part of the PD(D/E)XK superfamily but does not appear to have a full set of catalytic residues.


Pssm-ID: 375443  Cd Length: 125  Bit Score: 192.28  E-value: 4.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993    11 PVHVPLGHIVASEKWRGSQLAQEMQGKVRLIFEEGLASADFYLSSKSCILYVTEADLVAGHGYRKRLARFRNSSHLQGII 90
Cdd:pfam17949   1 NVSVPLGHILCSEKWRNSSLVQILKDKIKIIFEDRLGVVDFHPSNDTAIIYISEADIIAGNGYKRRLVKLRNANVFQGIV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 30519993    91 IVEKTQMSEQYFPAVQKFTVLDLGMVLLPVASQSEASCLIIHLVQ 135
Cdd:pfam17949  81 LAEKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 166-218 7.26e-13

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 61.39  E-value: 7.26e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30519993   166 IPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFTQPKRQQ 218
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPANRE 62
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
110-208 1.04e-11

ERCC4-type crossover junction endonuclease [Replication, recombination and repair];


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 61.73  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993 110 VLDLGMVLLPVASQSEASCLIIHLVQEQTREPSKNPFLRKKRS--MLSE--LSLVQTvqqIPGVGKVKAPLLLQKFPSIQ 185
Cdd:COG1948 103 ALDFGIPVLPTRDAEDTAELLVTLARREQEEEKREVSLHGKKKpkTLREqqLYVVES---LPGIGPKLARRLLEHFGSVE 179

                        90       100
                ....*....|....*....|....*
gi 30519993 186 QLSNASVQELEEV--VGPAAAQQIH 208
Cdd:COG1948 180 AVFNASEEELMKVegIGEKTAERIR 204
uvrC PRK00558
excinuclease ABC subunit UvrC;
147-211 5.64e-11

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 61.29  E-value: 5.64e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30519993  147 LRKKRSMLSELslvqtvQQIPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFF 211
Cdd:PRK00558 535 KRSKARLTSAL------DDIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVpgISKKLAEAIYEAL 595
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
166-218 5.12e-10

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 58.50  E-value: 5.12e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30519993 166 IPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFTQPKRQQ 218
Cdd:COG0272 517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFAEPHNRE 571
PRK13766 PRK13766
Hef nuclease; Provisional
 111-207 1.12e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.55  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  111 LDLGMVLLPVASQSEASCLIIHLVQ-EQ-TREPSKNPFLRKKRSMLSElslvqtvQQ------IPGVGKVKAPLLLQKFP 182
Cdd:PRK13766 664 VDFGIPILFTRDEEETADLLKVIAKrEQeEEKREVSVHGEKKAMTLKE-------QQeyivesLPDVGPVLARNLLEHFG 736

                         90       100
                 ....*....|....*....|....*..
gi 30519993  183 SIQQLSNASVQELEEV--VGPAAAQQI 207
Cdd:PRK13766 737 SVEAVMTASEEELMEVegIGEKTAKRI 763
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 17-139 5.83e-72

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


Pssm-ID: 410852  Cd Length: 123  Bit Score: 214.37  E-value: 5.83e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  17 GHIVASEKWRGSQLAQEMQGKVRLIFEEGLASADFYLSSKSCILYVTEADLVAGHGYRKRLARFRNSSHLQGIIIVEKTQ 96
Cdd:cd20076   1 GHILVNEKWRGSELVKSLQGKVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30519993  97 MSEQYFPAVQKFTVLDLGMVLLPVASQSEASCLIIHLVQEQTR 139
Cdd:cd20076  81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 11-135 4.10e-63

FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the FANCM protein. This domain is part of the PD(D/E)XK superfamily but does not appear to have a full set of catalytic residues.


Pssm-ID: 375443  Cd Length: 125  Bit Score: 192.28  E-value: 4.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993    11 PVHVPLGHIVASEKWRGSQLAQEMQGKVRLIFEEGLASADFYLSSKSCILYVTEADLVAGHGYRKRLARFRNSSHLQGII 90
Cdd:pfam17949   1 NVSVPLGHILCSEKWRNSSLVQILKDKIKIIFEDRLGVVDFHPSNDTAIIYISEADIIAGNGYKRRLVKLRNANVFQGIV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 30519993    91 IVEKTQMSEQYFPAVQKFTVLDLGMVLLPVASQSEASCLIIHLVQ 135
Cdd:pfam17949  81 LAEKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
XPF_nuclease-like cd19940
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
 18-135 3.51e-21

nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage.


Pssm-ID: 410849 [Multi-domain]  Cd Length: 126  Bit Score: 85.13  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  18 HIVASEKWRGSQLAQEMQG-KVRLIFEEgLASADFYLSSKSCILYVTEADLVAG---HGYRKRLARFRNSsHLQGIIIVE 93
Cdd:cd19940   1 SIVVDPRERRSELLSELQRlGVQVEFED-LAVGDYVLSNRTCVERKSLSDLVSSinkGRLREQLQRLTRK-FERRVLLVE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30519993  94 KTQ-------MSEQYFPAVQKFTVLDlGMVLLPVASQSEASCLIIHLVQ 135
Cdd:cd19940  79 KDRskfrsmvSSVQALSALTKLQLLT-GIRLLIVASPKETADLLEELTQ 126
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 166-218 7.26e-13

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 61.39  E-value: 7.26e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30519993   166 IPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFTQPKRQQ 218
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPANRE 62
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
110-208 1.04e-11

ERCC4-type crossover junction endonuclease [Replication, recombination and repair];


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 61.73  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993 110 VLDLGMVLLPVASQSEASCLIIHLVQEQTREPSKNPFLRKKRS--MLSE--LSLVQTvqqIPGVGKVKAPLLLQKFPSIQ 185
Cdd:COG1948 103 ALDFGIPVLPTRDAEDTAELLVTLARREQEEEKREVSLHGKKKpkTLREqqLYVVES---LPGIGPKLARRLLEHFGSVE 179

                        90       100
                ....*....|....*....|....*
gi 30519993 186 QLSNASVQELEEV--VGPAAAQQIH 208
Cdd:COG1948 180 AVFNASEEELMKVegIGEKTAERIR 204
uvrC PRK00558
excinuclease ABC subunit UvrC;
147-211 5.64e-11

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 61.29  E-value: 5.64e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30519993  147 LRKKRSMLSELslvqtvQQIPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFF 211
Cdd:PRK00558 535 KRSKARLTSAL------DDIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVpgISKKLAEAIYEAL 595
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
166-218 5.12e-10

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 58.50  E-value: 5.12e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30519993 166 IPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFTQPKRQQ 218
Cdd:COG0272 517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFAEPHNRE 571
ligA PRK14351
NAD-dependent DNA ligase LigA; Provisional
 136-212 2.92e-05

NAD-dependent DNA ligase LigA; Provisional


Pssm-ID: 184640 [Multi-domain]  Cd Length: 689  Bit Score: 44.36  E-value: 2.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30519993  136 EQTREPSKNPFLrkkrsmlSELSlvqtvqqIPGVGKVKAPLLLQKFPSIQQLSNASVQELEEV--VGPAAAQQIHTFFT 212
Cdd:PRK14351 517 EASREPPLADFL-------VALG-------IPEVGPTTARNLAREFGTFEAIMDADEEALRAVddVGPTVAEEIREFFD 581
PRK13766 PRK13766
Hef nuclease; Provisional
 111-207 1.12e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.55  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519993  111 LDLGMVLLPVASQSEASCLIIHLVQ-EQ-TREPSKNPFLRKKRSMLSElslvqtvQQ------IPGVGKVKAPLLLQKFP 182
Cdd:PRK13766 664 VDFGIPILFTRDEEETADLLKVIAKrEQeEEKREVSVHGEKKAMTLKE-------QQeyivesLPDVGPVLARNLLEHFG 736

                         90       100
                 ....*....|....*....|....*..
gi 30519993  183 SIQQLSNASVQELEEV--VGPAAAQQI 207
Cdd:PRK13766 737 SVEAVMTASEEELMEVegIGEKTAKRI 763
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH