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Conserved domains on  [gi|1676324279|dbj|BBD83878|]
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CG4364, partial [Drosophila fuyamai]

Protein Classification

NOP7 and BRCT_pescadillo_like domain-containing protein( domain architecture ID 13419910)

protein containing domains NOP7, BRCT_pescadillo_like, and PTZ00121

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BRCT_pescadillo_like cd17709
BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish ...
116-203 9.61e-56

BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish as a protein involved in the control of cell proliferation, specifically in the developing embryo. Mammalian homologs have been linked to ribosome biogenesis and nucleologenesis, and yeast homologs have been shown to be required for synthesis of the 60S ribosomal subunit. Pescadillo contains a BRCT domain.


:

Pssm-ID: 349341  Cd Length: 86  Bit Score: 176.61  E-value: 9.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 116 LFKGLKFFINREVPREPLVILIRSFGGKVSWDSSVFAGSayDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQR 195
Cdd:cd17709     1 LFKGLKFFLSREVPRESLEFIIRSFGGEVSWDGSDSPGA--DEDDESITHQIVDRPVQNKQYLSREYVQPQWVFDCVNAR 78

                  ....*...
gi 1676324279 196 QLLPTNKY 203
Cdd:cd17709    79 ILLPVEDY 86
NOP7 super family cl34924
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
5-283 3.40e-49

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5163:

Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 174.11  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279   5 EVDFKVMSIFVEFYTIMLGFTNFRLFHSLNLAYPPQF-----------PSSVLQDS-------EDSLKDEASFVSDRIAA 66
Cdd:COG5163   212 DVDFRIMLTFLEFYSTLLHFVSLKLYVEEGLDYPPKFdwskpnfldglSSYELEESsslpteiEEDVKVESLDSSTLKSA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279  67 LNFELLRTD--------KVQEDEEELDIDMELLEQDGD-SKRIIKMKQEAQEVARLRTLFKGLKFFINREVPREPLVILI 137
Cdd:COG5163   292 VCNDPGNIDvskeelseKIPELMVECRLVEEKLDTFEDnNKNKDIMEMVSKPCSSLKSLFSGFKFYISREVPGDSLEFII 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 138 RSFGGKVSWDSSVFAGSAYDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQRQLLPTNKYFLGEKLPPHLSPFV 217
Cdd:COG5163   372 LSCGGSVVGSPCEADIHVSEKVDEKVTHQIVDRPVMKNKVEGRTYIQPQWLFDSINKGKLACVENYCVGKRLPPHLSPFA 451
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324279 218 DSkrDTYIPPEEkaLLDPSLIETHAQSDDDSEDDAEKEEEETVDQ-----ELLDAQLQLAYQQETAEYKKY 283
Cdd:COG5163   452 SV--DSYDPRAS--LMTMEETQRHSEEDLVNRFEDVRYEHVAGEEdddddEELQAQKELELEAQGIKYSET 518
 
Name Accession Description Interval E-value
BRCT_pescadillo_like cd17709
BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish ...
116-203 9.61e-56

BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish as a protein involved in the control of cell proliferation, specifically in the developing embryo. Mammalian homologs have been linked to ribosome biogenesis and nucleologenesis, and yeast homologs have been shown to be required for synthesis of the 60S ribosomal subunit. Pescadillo contains a BRCT domain.


Pssm-ID: 349341  Cd Length: 86  Bit Score: 176.61  E-value: 9.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 116 LFKGLKFFINREVPREPLVILIRSFGGKVSWDSSVFAGSayDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQR 195
Cdd:cd17709     1 LFKGLKFFLSREVPRESLEFIIRSFGGEVSWDGSDSPGA--DEDDESITHQIVDRPVQNKQYLSREYVQPQWVFDCVNAR 78

                  ....*...
gi 1676324279 196 QLLPTNKY 203
Cdd:cd17709    79 ILLPVEDY 86
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
5-283 3.40e-49

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 174.11  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279   5 EVDFKVMSIFVEFYTIMLGFTNFRLFHSLNLAYPPQF-----------PSSVLQDS-------EDSLKDEASFVSDRIAA 66
Cdd:COG5163   212 DVDFRIMLTFLEFYSTLLHFVSLKLYVEEGLDYPPKFdwskpnfldglSSYELEESsslpteiEEDVKVESLDSSTLKSA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279  67 LNFELLRTD--------KVQEDEEELDIDMELLEQDGD-SKRIIKMKQEAQEVARLRTLFKGLKFFINREVPREPLVILI 137
Cdd:COG5163   292 VCNDPGNIDvskeelseKIPELMVECRLVEEKLDTFEDnNKNKDIMEMVSKPCSSLKSLFSGFKFYISREVPGDSLEFII 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 138 RSFGGKVSWDSSVFAGSAYDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQRQLLPTNKYFLGEKLPPHLSPFV 217
Cdd:COG5163   372 LSCGGSVVGSPCEADIHVSEKVDEKVTHQIVDRPVMKNKVEGRTYIQPQWLFDSINKGKLACVENYCVGKRLPPHLSPFA 451
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324279 218 DSkrDTYIPPEEkaLLDPSLIETHAQSDDDSEDDAEKEEEETVDQ-----ELLDAQLQLAYQQETAEYKKY 283
Cdd:COG5163   452 SV--DSYDPRAS--LMTMEETQRHSEEDLVNRFEDVRYEHVAGEEdddddEELQAQKELELEAQGIKYSET 518
Pescadillo_N pfam06732
Pescadillo N-terminus; This family represents the N-terminal region of Pescadillo. Pescadillo ...
4-59 3.86e-16

Pescadillo N-terminus; This family represents the N-terminal region of Pescadillo. Pescadillo protein localizes to distinct substructures of the interphase nucleus including nucleoli, the site of ribosome biogenesis. During mitosis pescadillo closely associates with the periphery of metaphase chromosomes and by late anaphase is associated with nucleolus-derived foci and prenucleolar bodies. Blastomeres in mouse embryos lacking pescadillo arrest at morula stages of development, the nucleoli fail to differentiate and accumulation of ribosomes is inhibited. It has been proposed that in mammalian cells pescadillo is essential for ribosome biogenesis and nucleologenesis and that disruption to its function results in cell cycle arrest. This family is often found in conjunction with a pfam00533 domain.


Pssm-ID: 461996  Cd Length: 269  Bit Score: 77.28  E-value: 3.86e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279   4 QEVDFKVMSIFVEFYTIMLGFTNFRLFHSLNLAYPPQFPSSVLQDSED----SLKDEASF 59
Cdd:pfam06732 205 TDVDFRVMLTFLEFYETLLGFVNFKLYHSLNLKYPPKLDPRKDEKAAGlaalSLESKAST 264
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
113-203 2.00e-13

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 65.08  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 113 LRTLFKGLKFFINR--EVPREPLVILIRSFGGKVSWDSsvfagsayDESDETITHQIVDRPSLATQYiSRDYVQPQWLFD 190
Cdd:pfam16589   1 LPNLFEPLRFYINAipSPSRSKLKRLIEANGGTVVDNI--------NPAVYIVIAPYNKTDKLAENT-KLGVVSPQWIFD 71
                          90
                  ....*....|...
gi 1676324279 191 CVNQRQLLPTNKY 203
Cdd:pfam16589  72 CVKKGKLLPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
116-192 8.05e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.21  E-value: 8.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279  116 LFKGLKFFINR---EVPREPLVILIRSFGGKVSWDSSVFagsaydesdeTITHQIVDRPSLATQYI------SRDYVQPQ 186
Cdd:smart00292   3 LFKGKTFYITGsfdKEERDELKELIEALGGKVTSSLSSK----------TTTHVIVGSPEGGKLELlkaialGIPIVKEE 72

                   ....*.
gi 1676324279  187 WLFDCV 192
Cdd:smart00292  73 WLLDCL 78
 
Name Accession Description Interval E-value
BRCT_pescadillo_like cd17709
BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish ...
116-203 9.61e-56

BRCT domain of pescadillo and related proteins; Pescadillo has been characterized in zebrafish as a protein involved in the control of cell proliferation, specifically in the developing embryo. Mammalian homologs have been linked to ribosome biogenesis and nucleologenesis, and yeast homologs have been shown to be required for synthesis of the 60S ribosomal subunit. Pescadillo contains a BRCT domain.


Pssm-ID: 349341  Cd Length: 86  Bit Score: 176.61  E-value: 9.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 116 LFKGLKFFINREVPREPLVILIRSFGGKVSWDSSVFAGSayDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQR 195
Cdd:cd17709     1 LFKGLKFFLSREVPRESLEFIIRSFGGEVSWDGSDSPGA--DEDDESITHQIVDRPVQNKQYLSREYVQPQWVFDCVNAR 78

                  ....*...
gi 1676324279 196 QLLPTNKY 203
Cdd:cd17709    79 ILLPVEDY 86
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
5-283 3.40e-49

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 174.11  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279   5 EVDFKVMSIFVEFYTIMLGFTNFRLFHSLNLAYPPQF-----------PSSVLQDS-------EDSLKDEASFVSDRIAA 66
Cdd:COG5163   212 DVDFRIMLTFLEFYSTLLHFVSLKLYVEEGLDYPPKFdwskpnfldglSSYELEESsslpteiEEDVKVESLDSSTLKSA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279  67 LNFELLRTD--------KVQEDEEELDIDMELLEQDGD-SKRIIKMKQEAQEVARLRTLFKGLKFFINREVPREPLVILI 137
Cdd:COG5163   292 VCNDPGNIDvskeelseKIPELMVECRLVEEKLDTFEDnNKNKDIMEMVSKPCSSLKSLFSGFKFYISREVPGDSLEFII 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 138 RSFGGKVSWDSSVFAGSAYDESDETITHQIVDRPSLATQYISRDYVQPQWLFDCVNQRQLLPTNKYFLGEKLPPHLSPFV 217
Cdd:COG5163   372 LSCGGSVVGSPCEADIHVSEKVDEKVTHQIVDRPVMKNKVEGRTYIQPQWLFDSINKGKLACVENYCVGKRLPPHLSPFA 451
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324279 218 DSkrDTYIPPEEkaLLDPSLIETHAQSDDDSEDDAEKEEEETVDQ-----ELLDAQLQLAYQQETAEYKKY 283
Cdd:COG5163   452 SV--DSYDPRAS--LMTMEETQRHSEEDLVNRFEDVRYEHVAGEEdddddEELQAQKELELEAQGIKYSET 518
Pescadillo_N pfam06732
Pescadillo N-terminus; This family represents the N-terminal region of Pescadillo. Pescadillo ...
4-59 3.86e-16

Pescadillo N-terminus; This family represents the N-terminal region of Pescadillo. Pescadillo protein localizes to distinct substructures of the interphase nucleus including nucleoli, the site of ribosome biogenesis. During mitosis pescadillo closely associates with the periphery of metaphase chromosomes and by late anaphase is associated with nucleolus-derived foci and prenucleolar bodies. Blastomeres in mouse embryos lacking pescadillo arrest at morula stages of development, the nucleoli fail to differentiate and accumulation of ribosomes is inhibited. It has been proposed that in mammalian cells pescadillo is essential for ribosome biogenesis and nucleologenesis and that disruption to its function results in cell cycle arrest. This family is often found in conjunction with a pfam00533 domain.


Pssm-ID: 461996  Cd Length: 269  Bit Score: 77.28  E-value: 3.86e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279   4 QEVDFKVMSIFVEFYTIMLGFTNFRLFHSLNLAYPPQFPSSVLQDSED----SLKDEASF 59
Cdd:pfam06732 205 TDVDFRVMLTFLEFYETLLGFVNFKLYHSLNLKYPPKLDPRKDEKAAGlaalSLESKAST 264
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
113-203 2.00e-13

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 65.08  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 113 LRTLFKGLKFFINR--EVPREPLVILIRSFGGKVSWDSsvfagsayDESDETITHQIVDRPSLATQYiSRDYVQPQWLFD 190
Cdd:pfam16589   1 LPNLFEPLRFYINAipSPSRSKLKRLIEANGGTVVDNI--------NPAVYIVIAPYNKTDKLAENT-KLGVVSPQWIFD 71
                          90
                  ....*....|...
gi 1676324279 191 CVNQRQLLPTNKY 203
Cdd:pfam16589  72 CVKKGKLLPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
116-192 8.05e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.21  E-value: 8.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279  116 LFKGLKFFINR---EVPREPLVILIRSFGGKVSWDSSVFagsaydesdeTITHQIVDRPSLATQYI------SRDYVQPQ 186
Cdd:smart00292   3 LFKGKTFYITGsfdKEERDELKELIEALGGKVTSSLSSK----------TTTHVIVGSPEGGKLELlkaialGIPIVKEE 72

                   ....*.
gi 1676324279  187 WLFDCV 192
Cdd:smart00292  73 WLLDCL 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
114-192 2.13e-06

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 44.98  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 114 RTLFKGLKFFINR--EVPREPLVILIRSFGGKVSwdssvfagsayDESDETITHQIVDRPSLA-TQYISR--DYVQPQWL 188
Cdd:pfam00533   3 EKLFSGKTFVITGldGLERDELKELIEKLGGKVT-----------DSLSKKTTHVIVEARTKKyLKAKELgiPIVTEEWL 71

                  ....
gi 1676324279 189 FDCV 192
Cdd:pfam00533  72 LDCI 75
BRCT_XRCC1_rpt2 cd17707
Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and ...
112-203 9.87e-06

Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This model corresponds to the second BRCT domain.


Pssm-ID: 349340  Cd Length: 94  Bit Score: 43.41  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 112 RLRTLFKGLKFFINREVP---REPLVILIRSFGGKVSWDSS-----VFAGSAYDES-DETIThqivDRPSLAtqyisrdY 182
Cdd:cd17707     1 ELPDFFSGKHFFLYGDFPadeRRLLKRYITAFNGEVEDYMSdkvtfVVTNQEWDDNfDEALA----ENPSLA-------F 69
                          90       100
                  ....*....|....*....|.
gi 1676324279 183 VQPQWLFDCVNQRQLLPTNKY 203
Cdd:cd17707    70 VRPRWIYACHEKQKLLPCQPY 90
BRCT_DNA_ligase_IV_rpt1 cd17722
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ...
116-205 2.23e-05

first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one.


Pssm-ID: 349354 [Multi-domain]  Cd Length: 90  Bit Score: 42.67  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 116 LFKGLKFFI----NREVPREPLVILIRSFGGKVSwdssvfagsAYDESDETIThqIVDRPS---LATQYISR--DYVQPQ 186
Cdd:cd17722     1 IFEGVEFCVmsdmSSPKSKAELEKLIKENGGKVV---------QNPGAPDTIC--VIAGREvvkVKNLIKSGghDVVKPS 69
                          90
                  ....*....|....*....
gi 1676324279 187 WLFDCVNQRQLLPTNKYFL 205
Cdd:cd17722    70 WLLDCIARKELLPLEPKYM 88
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
116-205 3.66e-04

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 39.09  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 116 LFKGLKFFIN--REVPREPLVILIRSFGGKVSwdssvfagsAYdESDETITHQIVDR--PSLATQYISRD---YVQPQWL 188
Cdd:cd17719     1 IFKGVVIYVNgyTDPSADELKRLILLHGGQYE---------HY-YSRSRVTHIIATNlpGSKIKKLKKARnykVVRPEWI 70
                          90
                  ....*....|....*..
gi 1676324279 189 FDCVNQRQLLPTNKYFL 205
Cdd:cd17719    71 VDSIKAGRLLPEAPYLL 87
LIG3_BRCT pfam16759
DNA ligase 3 BRCT domain; The BRCT domain of DNA ligase 3 (LIG3) binds to the C-terminal BRCT ...
112-195 2.01e-03

DNA ligase 3 BRCT domain; The BRCT domain of DNA ligase 3 (LIG3) binds to the C-terminal BRCT domain of the scaffolding protein X-ray repair cross-complementing protein 1 (XRCC1) and mediates homo- and heterodimerization.


Pssm-ID: 465260  Cd Length: 77  Bit Score: 36.58  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 112 RLRTLFKGLKFFINREVP-REPLVILIRSFGGKVswdssvfagsaYDESDE-TITHQIVDRPSLATQYISRD--YVQPQW 187
Cdd:pfam16759   1 PLPDIFTGVRLFLPPSVPdFSKLRRYFIAYDGDL-----------VQEYDLdSATHVVVPKDSAKEKEESSGakHVTASW 69

                  ....*...
gi 1676324279 188 LFDCVNQR 195
Cdd:pfam16759  70 IWECIKKR 77
BRCT_DNA_ligase_III cd18431
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ...
117-199 2.18e-03

BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.


Pssm-ID: 349384 [Multi-domain]  Cd Length: 78  Bit Score: 36.52  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 117 FKGLKFFINREVP--REPLVILIRSFGGKVSwdssvfagsAYDESDETiTHQIVDRPSLAtQYISRDYVQPQWLFDCVNQ 194
Cdd:cd18431     5 FTGVKVYLPGSVEddYKKLKRYFIAYDGDVV---------EEYDEEDA-THVVVDRDDKL-GNPSAKVVSPEWLWDCIKK 73

                  ....*
gi 1676324279 195 RQLLP 199
Cdd:cd18431    74 QKLVP 78
BRCT_TopBP1_rpt3 cd17718
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
153-196 2.98e-03

third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.


Pssm-ID: 349350  Cd Length: 83  Bit Score: 36.42  E-value: 2.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1676324279 153 GSAYDESDETITHQIV--DRPSLATQY---ISRDY-VQPQWLFDCVNQRQ 196
Cdd:cd17718    34 GTRFNQLNESVTHVVVgeSSEELLKELaklAGRPHvVTPSWLLECFKQGK 83
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
114-194 9.41e-03

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 34.52  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324279 114 RTLF-KGLKFFI--NREVPREPLVILIRSFGGKVSWDSSvfagsaydESDETIThQIVDRPSlatqyisRDYVQPQWLFD 190
Cdd:cd17751     5 QNLFaDGGPIYVssNSVPPKDKLEELVLLCGGKVVKSSR--------KADICIG-KTPPNPD-------KPSVSEKWLLD 68

                  ....
gi 1676324279 191 CVNQ 194
Cdd:cd17751    69 SITN 72
 
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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