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Conserved domains on  [gi|530381539|ref|XP_005248944|]
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Fanconi anemia group E protein isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FANCE_c-term super family cl12008
Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an ...
274-493 4.40e-118

Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an autosomal recessive disorder associated with increased susceptibility to various cancers, bone marrow failure, cardiac, renal, and limb malformations, and other characteristics. Cells are highly sensitive to DNA damaging agents. A multi-subunit protein complex, the FA core complex, is responsible for ubiquitination of the protein FANCD2 in response to DNA damage. This monoubiquitination results in a downstream effect on homology-directed DNA repair. FANCE is part of the FA core complex and its C-terminal domain, which is modeled here, has been shown to directly interact with FANCD2. The domain contains a five-fold repeat of a structural unit similar to ARM and HEAT repeats. FANCE appears conserved in metazoa and in plants.


The actual alignment was detected with superfamily member pfam11510:

Pssm-ID: 299861  Cd Length: 262  Bit Score: 347.40  E-value: 4.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  274 LAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSP 353
Cdd:pfam11510   1 LAESKELPDAIKAALPRIKELLDAEEEGLEGLDDAPPSALKLLHECDPNEMDLLCAQLCLPELSDLGLLQFCSCLLALSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  354 DLSLSNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKMESLEPDA 433
Cdd:pfam11510  81 DLSHSNASALIRHLFLGKILSLAEPASRCLTTALTSFAAKYPRPTCQALIDPLLQAGGLGPAQADLLCCLVKIDCLEPDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  434 QVLMLGQILELPWKEETFLVLQSLLERQ------------------------------------------ITETQRLGLA 471
Cdd:pfam11510 161 QLLMFGQALEAPWDEETFLVIHALLDRKlelspedfclfaehlckkglaasksmafaklllsvltkyqanINEACHHGLA 240
                         250       260
                  ....*....|....*....|..
gi 530381539  472 MALEPNTTFLRKSLKAALKHLG 493
Cdd:pfam11510 241 MALEFNETFLKKSLKAALKHIG 262
 
Name Accession Description Interval E-value
FA_FANCE pfam11510
Fanconi Anaemia group E protein FANCE; Fanconi Anaemia (FA) is a cancer predisposition ...
274-493 4.40e-118

Fanconi Anaemia group E protein FANCE; Fanconi Anaemia (FA) is a cancer predisposition disorder. In response to DNA damage, the FA core complex monoubiquitinates the downatream FANCD2 protein. The protein FANCE has an important role in DNA repair as it is the FANCD2-binding protein in the FA core complex so it represents the link between the FA core complex and FANCD2. The sequence shown is the C terminal domain of the protein which consists predominantly of helices and does not contain any beta-strand. The fold of the polypeptide is a continuous right-handed solenoidal pattern from the N terminal to the C terminal end.


Pssm-ID: 288377  Cd Length: 262  Bit Score: 347.40  E-value: 4.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  274 LAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSP 353
Cdd:pfam11510   1 LAESKELPDAIKAALPRIKELLDAEEEGLEGLDDAPPSALKLLHECDPNEMDLLCAQLCLPELSDLGLLQFCSCLLALSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  354 DLSLSNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKMESLEPDA 433
Cdd:pfam11510  81 DLSHSNASALIRHLFLGKILSLAEPASRCLTTALTSFAAKYPRPTCQALIDPLLQAGGLGPAQADLLCCLVKIDCLEPDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  434 QVLMLGQILELPWKEETFLVLQSLLERQ------------------------------------------ITETQRLGLA 471
Cdd:pfam11510 161 QLLMFGQALEAPWDEETFLVIHALLDRKlelspedfclfaehlckkglaasksmafaklllsvltkyqanINEACHHGLA 240
                         250       260
                  ....*....|....*....|..
gi 530381539  472 MALEPNTTFLRKSLKAALKHLG 493
Cdd:pfam11510 241 MALEFNETFLKKSLKAALKHIG 262
FANCE_c-term cd07439
Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an ...
278-491 1.76e-69

Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an autosomal recessive disorder associated with increased susceptibility to various cancers, bone marrow failure, cardiac, renal, and limb malformations, and other characteristics. Cells are highly sensitive to DNA damaging agents. A multi-subunit protein complex, the FA core complex, is responsible for ubiquitination of the protein FANCD2 in response to DNA damage. This monoubiquitination results in a downstream effect on homology-directed DNA repair. FANCE is part of the FA core complex and its C-terminal domain, which is modeled here, has been shown to directly interact with FANCD2. The domain contains a five-fold repeat of a structural unit similar to ARM and HEAT repeats. FANCE appears conserved in metazoa and in plants.


Pssm-ID: 143633  Cd Length: 254  Bit Score: 222.21  E-value: 1.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 278 LELPKAIQDQLPRLQQLLKTLEEGLegleDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSPDLSL 357
Cdd:cd07439    1 AELPSVIQEVLEDIKELLLQEGEWL----PSSPDELQFLHSCSPSQMEVLCSQLQLSSLSDQTLLLLCSSLLPLSPDLSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 358 SNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKmESLEPDAQVLM 437
Cdd:cd07439   77 ANAVVFTRHLLLPKLLSLNESASRALVAALASFAKRYPRPFCEALLRPLLQCPHPGPFQAELLCRLVK-ECFEPDAVLLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 438 LGQILELP---WKEETFLVLQSLLER------------------------------------------QITETQRLGLAM 472
Cdd:cd07439  156 LHQILISPnlvWTEETFTVIQALLNRkpplseesfselvsklqeqaeafskslkfaklllavitkygpQMSPAHKQSLSE 235
                        250
                 ....*....|....*....
gi 530381539 473 ALEPNTTFLRKSLKAALKH 491
Cdd:cd07439  236 ALERNKTFLKKSILAALKR 254
 
Name Accession Description Interval E-value
FA_FANCE pfam11510
Fanconi Anaemia group E protein FANCE; Fanconi Anaemia (FA) is a cancer predisposition ...
274-493 4.40e-118

Fanconi Anaemia group E protein FANCE; Fanconi Anaemia (FA) is a cancer predisposition disorder. In response to DNA damage, the FA core complex monoubiquitinates the downatream FANCD2 protein. The protein FANCE has an important role in DNA repair as it is the FANCD2-binding protein in the FA core complex so it represents the link between the FA core complex and FANCD2. The sequence shown is the C terminal domain of the protein which consists predominantly of helices and does not contain any beta-strand. The fold of the polypeptide is a continuous right-handed solenoidal pattern from the N terminal to the C terminal end.


Pssm-ID: 288377  Cd Length: 262  Bit Score: 347.40  E-value: 4.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  274 LAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSP 353
Cdd:pfam11510   1 LAESKELPDAIKAALPRIKELLDAEEEGLEGLDDAPPSALKLLHECDPNEMDLLCAQLCLPELSDLGLLQFCSCLLALSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  354 DLSLSNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKMESLEPDA 433
Cdd:pfam11510  81 DLSHSNASALIRHLFLGKILSLAEPASRCLTTALTSFAAKYPRPTCQALIDPLLQAGGLGPAQADLLCCLVKIDCLEPDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539  434 QVLMLGQILELPWKEETFLVLQSLLERQ------------------------------------------ITETQRLGLA 471
Cdd:pfam11510 161 QLLMFGQALEAPWDEETFLVIHALLDRKlelspedfclfaehlckkglaasksmafaklllsvltkyqanINEACHHGLA 240
                         250       260
                  ....*....|....*....|..
gi 530381539  472 MALEPNTTFLRKSLKAALKHLG 493
Cdd:pfam11510 241 MALEFNETFLKKSLKAALKHIG 262
FANCE_c-term cd07439
Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an ...
278-491 1.76e-69

Fanconi anemia complementation group E protein, C-terminal domain; Fanconi Anemia (FA) is an autosomal recessive disorder associated with increased susceptibility to various cancers, bone marrow failure, cardiac, renal, and limb malformations, and other characteristics. Cells are highly sensitive to DNA damaging agents. A multi-subunit protein complex, the FA core complex, is responsible for ubiquitination of the protein FANCD2 in response to DNA damage. This monoubiquitination results in a downstream effect on homology-directed DNA repair. FANCE is part of the FA core complex and its C-terminal domain, which is modeled here, has been shown to directly interact with FANCD2. The domain contains a five-fold repeat of a structural unit similar to ARM and HEAT repeats. FANCE appears conserved in metazoa and in plants.


Pssm-ID: 143633  Cd Length: 254  Bit Score: 222.21  E-value: 1.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 278 LELPKAIQDQLPRLQQLLKTLEEGLegleDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSPDLSL 357
Cdd:cd07439    1 AELPSVIQEVLEDIKELLLQEGEWL----PSSPDELQFLHSCSPSQMEVLCSQLQLSSLSDQTLLLLCSSLLPLSPDLSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 358 SNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKmESLEPDAQVLM 437
Cdd:cd07439   77 ANAVVFTRHLLLPKLLSLNESASRALVAALASFAKRYPRPFCEALLRPLLQCPHPGPFQAELLCRLVK-ECFEPDAVLLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381539 438 LGQILELP---WKEETFLVLQSLLER------------------------------------------QITETQRLGLAM 472
Cdd:cd07439  156 LHQILISPnlvWTEETFTVIQALLNRkpplseesfselvsklqeqaeafskslkfaklllavitkygpQMSPAHKQSLSE 235
                        250
                 ....*....|....*....
gi 530381539 473 ALEPNTTFLRKSLKAALKH 491
Cdd:cd07439  236 ALERNKTFLKKSILAALKR 254
 
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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