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Conserved domains on  [gi|530417534|ref|XP_005259450|]
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Fanconi anemia core complex-associated protein 24 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 12-95 3.50e-48

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: 152.36  E-value: 3.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  12 RCCILYVTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 91
Cdd:cd20076   40 DCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVN 119


                 ....
gi 530417534  92 EQTK 95
Cdd:cd20076  120 EETK 123
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 123-172 2.17e-11

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: 56.38  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530417534  123 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 172
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPA 59
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 12-95 3.50e-48

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: 152.36  E-value: 3.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  12 RCCILYVTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 91
Cdd:cd20076   40 DCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVN 119


                 ....
gi 530417534  92 EQTK 95
Cdd:cd20076  120 EETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 12-91 2.27e-42

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: 137.58  E-value: 2.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534   12 RCCILYVTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 91
Cdd:pfam17949  46 DTAIIYISEADIIAGNGYKRRLVKLRNANVFQGIVLAEKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 123-172 2.17e-11

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: 56.38  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530417534  123 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 172
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPA 59
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
66-171 3.79e-11

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


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 59.03  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  66 VLDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEpSLLRTVQQIPGVGKVKAPLLLQKFPSIQQL 144
Cdd:COG1948  103 ALDFGIPVLPTRDAEDtAELLVTLARREQEEEKREVSLHGKKKPKTLRE-QQLYVVESLPGIGPKLARRLLEHFGSVEAV 181

                         90       100
                 ....*....|....*....|....*....
gi 530417534 145 SNASIGELEQV--VGQAVAQQIHAFFTQP 171
Cdd:COG1948  182 FNASEEELMKVegIGEKTAERIREVLDSE 210
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
123-172 2.40e-09

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 55.03  E-value: 2.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530417534 123 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 172
Cdd:COG0272  517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFAEPH 568
uvrC PRK00558
excinuclease ABC subunit UvrC;
122-168 6.59e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 53.97  E-value: 6.59e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530417534 122 QIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFF 168
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVpgISKKLAEAIYEAL 595
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 12-95 3.50e-48

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: 152.36  E-value: 3.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  12 RCCILYVTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 91
Cdd:cd20076   40 DCAVIYISEADLVAGNGYKRKLVKLRKANYLRGIVIAEKTPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVN 119


                 ....
gi 530417534  92 EQTK 95
Cdd:cd20076  120 EETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 12-91 2.27e-42

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: 137.58  E-value: 2.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534   12 RCCILYVTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 91
Cdd:pfam17949  46 DTAIIYISEADIIAGNGYKRRLVKLRNANVFQGIVLAEKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
XPF_nuclease-like cd19940
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
 11-91 9.46e-17

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: 72.03  E-value: 9.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  11 ARCCILYVTEADLVAG---NGYRKRLVRVRNsNNLKGIVVVEKTR-------MSEQYFPALQKFTVLDlGMVLLPVASQM 80
Cdd:cd19940   38 NRTCVERKSLSDLVSSinkGRLREQLQRLTR-KFERRVLLVEKDRskfrsmvSSVQALSALTKLQLLT-GIRLLIVASPK 115

                         90
                 ....*....|.
gi 530417534  81 EASCLVIQLVQ 91
Cdd:cd19940  116 ETADLLEELTQ 126
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 123-172 2.17e-11

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: 56.38  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530417534  123 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 172
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPA 59
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
66-171 3.79e-11

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


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 59.03  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417534  66 VLDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEpSLLRTVQQIPGVGKVKAPLLLQKFPSIQQL 144
Cdd:COG1948  103 ALDFGIPVLPTRDAEDtAELLVTLARREQEEEKREVSLHGKKKPKTLRE-QQLYVVESLPGIGPKLARRLLEHFGSVEAV 181

                         90       100
                 ....*....|....*....|....*....
gi 530417534 145 SNASIGELEQV--VGQAVAQQIHAFFTQP 171
Cdd:COG1948  182 FNASEEELMKVegIGEKTAERIREVLDSE 210
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
123-172 2.40e-09

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 55.03  E-value: 2.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530417534 123 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 172
Cdd:COG0272  517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFAEPH 568
uvrC PRK00558
excinuclease ABC subunit UvrC;
122-168 6.59e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 53.97  E-value: 6.59e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530417534 122 QIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFF 168
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVpgISKKLAEAIYEAL 595
PRK13766 PRK13766
Hef nuclease; Provisional
 92-164 9.64e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 41.78  E-value: 9.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530417534  92 EQTKEPSKNPLLGKKRALLLSEPSLLrTVQQIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQI 164
Cdd:PRK13766 690 EQEEEKREVSVHGEKKAMTLKEQQEY-IVESLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVegIGEKTAKRI 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.
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