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Conserved domains on  [gi|665821158|ref|NP_001287907|]
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Fanconi anemia core complex-associated protein 24 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XPF_nuclease-like super family cl41760
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
 1-43 8.10e-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.


The actual alignment was detected with superfamily member cd20076:

Pssm-ID: 425391  Cd Length: 123  Bit Score: 80.71  E-value: 8.10e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665821158   1 MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQEQTK 43
Cdd:cd20076   81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
MUS81 super family cl34381
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
14-119 2.64e-12

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


The actual alignment was detected with superfamily member COG1948:

Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 60.58  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821158  14 VLDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEpSLLRTVQQIPGVGKVKAPLLLQKFPSIQQL 92
Cdd:COG1948  103 ALDFGIPVLPTRDAEDtAELLVTLARREQEEEKREVSLHGKKKPKTLRE-QQLYVVESLPGIGPKLARRLLEHFGSVEAV 181

                         90       100
                 ....*....|....*....|....*....
gi 665821158  93 SNASIGELEQV--VGQAVAQQIHAFFTQP 119
Cdd:COG1948  182 FNASEEELMKVegIGEKTAERIREVLDSE 210
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 1-43 8.10e-21

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: 80.71  E-value: 8.10e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665821158   1 MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQEQTK 43
Cdd:cd20076   81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 1-39 1.04e-16

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: 70.17  E-value: 1.04e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 665821158    1 MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 39
Cdd:pfam17949  87 LSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
14-119 2.64e-12

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


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 60.58  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821158  14 VLDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEpSLLRTVQQIPGVGKVKAPLLLQKFPSIQQL 92
Cdd:COG1948  103 ALDFGIPVLPTRDAEDtAELLVTLARREQEEEKREVSLHGKKKPKTLRE-QQLYVVESLPGIGPKLARRLLEHFGSVEAV 181

                         90       100
                 ....*....|....*....|....*....
gi 665821158  93 SNASIGELEQV--VGQAVAQQIHAFFTQP 119
Cdd:COG1948  182 FNASEEELMKVegIGEKTAERIREVLDSE 210
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 71-120 4.22e-12

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: 56.76  E-value: 4.22e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821158   71 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 120
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPA 59
uvrC PRK00558
excinuclease ABC subunit UvrC;
70-116 1.37e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 53.97  E-value: 1.37e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 665821158  70 QIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFF 116
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 ...
 1-43 8.10e-21

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: 80.71  E-value: 8.10e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665821158   1 MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQEQTK 43
Cdd:cd20076   81 MSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 1-39 1.04e-16

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: 70.17  E-value: 1.04e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 665821158    1 MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQ 39
Cdd:pfam17949  87 LSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
14-119 2.64e-12

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


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 60.58  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821158  14 VLDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEpSLLRTVQQIPGVGKVKAPLLLQKFPSIQQL 92
Cdd:COG1948  103 ALDFGIPVLPTRDAEDtAELLVTLARREQEEEKREVSLHGKKKPKTLRE-QQLYVVESLPGIGPKLARRLLEHFGSVEAV 181

                         90       100
                 ....*....|....*....|....*....
gi 665821158  93 SNASIGELEQV--VGQAVAQQIHAFFTQP 119
Cdd:COG1948  182 FNASEEELMKVegIGEKTAERIREVLDSE 210
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 71-120 4.22e-12

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: 56.76  E-value: 4.22e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821158   71 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 120
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFADPA 59
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
71-120 3.32e-10

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 55.80  E-value: 3.32e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665821158  71 IPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFFTQPR 120
Cdd:COG0272  517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFAEPH 568
uvrC PRK00558
excinuclease ABC subunit UvrC;
70-116 1.37e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 53.97  E-value: 1.37e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 665821158  70 QIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQV--VGQAVAQQIHAFF 116
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVpgISKKLAEAIYEAL 595
XPF_nuclease-like cd19940
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
 1-39 1.24e-06

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: 43.91  E-value: 1.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 665821158   1 MSEQYFPALQKFTVLDlGMVLLPVASQMEASCLVIQLVQ 39
Cdd:cd19940   89 SSVQALSALTKLQLLT-GIRLLIVASPKETADLLEELTQ 126
PRK13766 PRK13766
Hef nuclease; Provisional
 15-112 1.83e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.17  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821158  15 LDLGMVLLPVASQME-ASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEPSLLrTVQQIPGVGKVKAPLLLQKFPSIQQLS 93
Cdd:PRK13766 664 VDFGIPILFTRDEEEtADLLKVIAKREQEEEKREVSVHGEKKAMTLKEQQEY-IVESLPDVGPVLARNLLEHFGSVEAVM 742

                         90       100
                 ....*....|....*....|.
gi 665821158  94 NASIGELEQV--VGQAVAQQI 112
Cdd:PRK13766 743 TASEEELMEVegIGEKTAKRI 763
HHH_5 pfam14520
Helix-hairpin-helix domain;
66-112 5.41e-03

Helix-hairpin-helix domain;


Pssm-ID: 434010 [Multi-domain]  Cd Length: 57  Bit Score: 32.85  E-value: 5.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821158   66 RTVQQIPGVGKVKAPLLLQK-FPSIQQLSNASIGELEQV--VGQAVAQQI 112
Cdd:pfam14520   2 EELLSISGIGPKTALALLSAgIGTVEDLAEADVDELAEIpgIGEKTAQRI 51
 
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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