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Conserved domains on  [gi|392922079|ref|NP_506722|]
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BRCT domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WSN smart00453
Worm-specific (usually) N-terminal domain;
23-91 2.83e-20

Worm-specific (usually) N-terminal domain;


:

Pssm-ID: 197734  Cd Length: 69  Bit Score: 85.71  E-value: 2.83e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392922079     23 SNLQLISEDFRILSRVTNAISLQAGAIRKNIKVRDLLVELIRMPRDQFNNIIDVDIKVARTELNRMGEE 91
Cdd:smart00453    1 SKLQTVIERLSMLARVTNAISLQAGLINGSIPIDDVIAELLNIDSSKLSDIINVDLTKIDEGLNKLKEI 69
BRCT smart00292
breast cancer carboxy-terminal domain;
991-1063 4.85e-09

breast cancer carboxy-terminal domain;


:

Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.30  E-value: 4.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079    991 FHIWIDERTDINITNQFMEKFQAITSDEANS----NTTHVIVKTDENGALEtdsldLLLWVFNGAIIVKEQWMVDCL 1063
Cdd:smart00292    7 KTFYITGSFDKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPEGGKLE-----LLKAIALGIPIVKEEWLLDCL 78
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
872-947 1.97e-08

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079  872 NQDGKNTLLDAVREiNKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTPEQM 947
Cdd:COG0666   150 DNDGNTPLHLAAAN-GNLEIVKLlLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 469-667 3.33e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   469 TIKSFfdEYYKKLSNEIEKQKVNKTNSLRVKTRLKIIIDQIDKREVDFHNFMTHLSQNLKNIKVITNKSLpndtkidKLL 548
Cdd:TIGR01612 1241 MIKAM--EAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSL-------KII 1311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   549 VEMLDTSQLRGISKCLSQEFMQPLRVLEVIEAMITvrQFAGNKTVLKMNQYLDELAKVKNQLWKVEKQIKLITSQSNSSH 628
Cdd:TIGR01612 1312 EDFSEESDINDIKKELQKNLLDAQKHNSDINLYLN--EIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSE 1389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 392922079   629 NLVLKLKTpelfTASLGTCAHVLE------DLEEARQNHQLLSNY 667
Cdd:TIGR01612 1390 KLIKKIKD----DINLEECKSKIEstlddkDIDECIKKIKELKNH 1430
 
Name Accession Description Interval E-value
WSN smart00453
Worm-specific (usually) N-terminal domain;
23-91 2.83e-20

Worm-specific (usually) N-terminal domain;


Pssm-ID: 197734  Cd Length: 69  Bit Score: 85.71  E-value: 2.83e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392922079     23 SNLQLISEDFRILSRVTNAISLQAGAIRKNIKVRDLLVELIRMPRDQFNNIIDVDIKVARTELNRMGEE 91
Cdd:smart00453    1 SKLQTVIERLSMLARVTNAISLQAGLINGSIPIDDVIAELLNIDSSKLSDIINVDLTKIDEGLNKLKEI 69
WSN pfam02206
Domain of unknown function;
24-88 1.03e-16

Domain of unknown function;


Pssm-ID: 426657  Cd Length: 66  Bit Score: 75.57  E-value: 1.03e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392922079    24 NLQLISEDFRILSRVTNAISLQAGAIRKNIKVRDLLVELIRMPRDQFNNIIDVDIKVARTELNRM 88
Cdd:pfam02206    1 NLSLIVEKLSILARITNAISLQAGLIDGSIPVDDVISELLNLGSVTLSDIIKIDVDKLKELLEKL 65
BRCT smart00292
breast cancer carboxy-terminal domain;
991-1063 4.85e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.30  E-value: 4.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079    991 FHIWIDERTDINITNQFMEKFQAITSDEANS----NTTHVIVKTDENGALEtdsldLLLWVFNGAIIVKEQWMVDCL 1063
Cdd:smart00292    7 KTFYITGSFDKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPEGGKLE-----LLKAIALGIPIVKEEWLLDCL 78
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
872-947 1.97e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079  872 NQDGKNTLLDAVREiNKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTPEQM 947
Cdd:COG0666   150 DNDGNTPLHLAAAN-GNLEIVKLlLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 998-1072 2.79e-07

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 49.65  E-value: 2.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392922079  998 RTDINITNQFMEKFQAITSDEANSNTTHVIVKTDENGALETdSLDLLLWVFNGAIIVKEQWMVDCLENETVIEQD 1072
Cdd:cd17735    10 PEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCER-TLKYFLGIAGRKWVVSYQWITQSIKEGKILPEH 83
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 981-1063 1.11e-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: 47.29  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   981 NVPQKFPTTSFHIWIDERTDINITNQFMEKFQAITSDEANSNTTHVIVktdengalETDSLDLLLWVFNGAIIVKEQWMV 1060
Cdd:pfam00533    1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--------EARTKKYLKAKELGIPIVTEEWLL 72


                   ...
gi 392922079  1061 DCL 1063
Cdd:pfam00533   73 DCI 75
PHA03095 PHA03095
ankyrin-like protein; Provisional
 895-944 6.85e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 6.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392922079  895 VKAGSYINAFNKFGNTALHT--ATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTP 155
Ank_2 pfam12796
Ankyrin repeats (3 copies);
866-933 1.12e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392922079   866 YSLFLDNQDGKNTLLDAVREiNKTNAVNAVKAGSYINAFNKfGNTALHTATKSALPEIVKLLIKNGAD 933
Cdd:pfam12796   21 ADANLQDKNGRTALHLAAKN-GHLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 469-667 3.33e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   469 TIKSFfdEYYKKLSNEIEKQKVNKTNSLRVKTRLKIIIDQIDKREVDFHNFMTHLSQNLKNIKVITNKSLpndtkidKLL 548
Cdd:TIGR01612 1241 MIKAM--EAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSL-------KII 1311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   549 VEMLDTSQLRGISKCLSQEFMQPLRVLEVIEAMITvrQFAGNKTVLKMNQYLDELAKVKNQLWKVEKQIKLITSQSNSSH 628
Cdd:TIGR01612 1312 EDFSEESDINDIKKELQKNLLDAQKHNSDINLYLN--EIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSE 1389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 392922079   629 NLVLKLKTpelfTASLGTCAHVLE------DLEEARQNHQLLSNY 667
Cdd:TIGR01612 1390 KLIKKIKD----DINLEECKSKIEstlddkDIDECIKKIKELKNH 1430
 
Name Accession Description Interval E-value
WSN smart00453
Worm-specific (usually) N-terminal domain;
23-91 2.83e-20

Worm-specific (usually) N-terminal domain;


Pssm-ID: 197734  Cd Length: 69  Bit Score: 85.71  E-value: 2.83e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392922079     23 SNLQLISEDFRILSRVTNAISLQAGAIRKNIKVRDLLVELIRMPRDQFNNIIDVDIKVARTELNRMGEE 91
Cdd:smart00453    1 SKLQTVIERLSMLARVTNAISLQAGLINGSIPIDDVIAELLNIDSSKLSDIINVDLTKIDEGLNKLKEI 69
WSN pfam02206
Domain of unknown function;
24-88 1.03e-16

Domain of unknown function;


Pssm-ID: 426657  Cd Length: 66  Bit Score: 75.57  E-value: 1.03e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392922079    24 NLQLISEDFRILSRVTNAISLQAGAIRKNIKVRDLLVELIRMPRDQFNNIIDVDIKVARTELNRM 88
Cdd:pfam02206    1 NLSLIVEKLSILARITNAISLQAGLIDGSIPVDDVISELLNLGSVTLSDIIKIDVDKLKELLEKL 65
BRCT smart00292
breast cancer carboxy-terminal domain;
991-1063 4.85e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.30  E-value: 4.85e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079    991 FHIWIDERTDINITNQFMEKFQAITSDEANS----NTTHVIVKTDENGALEtdsldLLLWVFNGAIIVKEQWMVDCL 1063
Cdd:smart00292    7 KTFYITGSFDKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPEGGKLE-----LLKAIALGIPIVKEEWLLDCL 78
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
872-947 1.97e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079  872 NQDGKNTLLDAVREiNKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTPEQM 947
Cdd:COG0666   150 DNDGNTPLHLAAAN-GNLEIVKLlLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
872-944 7.86e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 7.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392922079  872 NQDGKNTLLDAVREiNKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:COG0666   117 DKDGETPLHLAAYN-GNLEIVKLlLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
872-944 1.74e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392922079  872 NQDGKNTLLDAVREINKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLlLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 998-1072 2.79e-07

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 49.65  E-value: 2.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392922079  998 RTDINITNQFMEKFQAITSDEANSNTTHVIVKTDENGALETdSLDLLLWVFNGAIIVKEQWMVDCLENETVIEQD 1072
Cdd:cd17735    10 PEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCER-TLKYFLGIAGRKWVVSYQWITQSIKEGKILPEH 83
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 981-1063 1.11e-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: 47.29  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   981 NVPQKFPTTSFHIWIDERTDINITNQFMEKFQAITSDEANSNTTHVIVktdengalETDSLDLLLWVFNGAIIVKEQWMV 1060
Cdd:pfam00533    1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--------EARTKKYLKAKELGIPIVTEEWLL 72


                   ...
gi 392922079  1061 DCL 1063
Cdd:pfam00533   73 DCI 75
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 1005-1069 3.14e-06

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 46.05  E-value: 3.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392922079 1005 NQFMEKFQAITSDEANSNTTHVIVKTDENGAlETDSLDLLLWVFNGAIIVKEQWMVDCLENETVI 1069
Cdd:cd17734    17 EKLAQLLKAKVVTEFSPEVTHVVVPADERGV-CPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 895-944 6.85e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 6.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392922079  895 VKAGSYINAFNKFGNTALHT--ATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTP 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
868-944 1.71e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 1.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079  868 LFLDNQDGKNTLLDAVREINKTNAVNAVKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
Ank_2 pfam12796
Ankyrin repeats (3 copies);
866-933 1.12e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392922079   866 YSLFLDNQDGKNTLLDAVREiNKTNAVNAVKAGSYINAFNKfGNTALHTATKSALPEIVKLLIKNGAD 933
Cdd:pfam12796   21 ADANLQDKNGRTALHLAAKN-GHLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86
Ank_5 pfam13857
Ankyrin repeats (many copies);
901-944 1.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 392922079   901 INAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 907-933 1.20e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.20e-03
                           10        20
                   ....*....|....*....|....*..
gi 392922079   907 FGNTALHTATKSALPEIVKLLIKNGAD 933
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 874-955 1.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079  874 DGKNTLLDAVREINKTNAVNAVKAGSYIN-AFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTmNRTPEQMIPLVY 952
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNT-DKFSPLHLAVMM 145


                  ...
gi 392922079  953 KDI 955
Cdd:PHA02875  146 GDI 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 877-944 2.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 2.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392922079  877 NTLLDAVREINKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKNGADRELLNTMNRTP 944
Cdd:PHA03100  160 KLLIDKGVDINAKNRVNYlLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 908-938 2.22e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 392922079   908 GNTALHTATKSA-LPEIVKLLIKNGADRELLN 938
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 852-955 3.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079  852 YYVGKPVHYENRWRYSLFLdnqdgkNTLLDAVREINK---------------TNAVNAVKA----GSYINAFNKFGNTAL 912
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVII------NTLLDYGADIEAlsqkigtalhfalcgTNPYMSVKTlidrGANVNSKNKDLSTPL 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 392922079  913 HTATK-SALPEIVKLLIKNGADRELLNTMNRTPeQMIPLVYKDI 955
Cdd:PHA02876  447 HYACKkNCKLDVIEMLLDNGADVNAINIQNQYP-LLIALEYHGI 489
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 469-667 3.33e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   469 TIKSFfdEYYKKLSNEIEKQKVNKTNSLRVKTRLKIIIDQIDKREVDFHNFMTHLSQNLKNIKVITNKSLpndtkidKLL 548
Cdd:TIGR01612 1241 MIKAM--EAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSL-------KII 1311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392922079   549 VEMLDTSQLRGISKCLSQEFMQPLRVLEVIEAMITvrQFAGNKTVLKMNQYLDELAKVKNQLWKVEKQIKLITSQSNSSH 628
Cdd:TIGR01612 1312 EDFSEESDINDIKKELQKNLLDAQKHNSDINLYLN--EIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSE 1389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 392922079   629 NLVLKLKTpelfTASLGTCAHVLE------DLEEARQNHQLLSNY 667
Cdd:TIGR01612 1390 KLIKKIKD----DINLEECKSKIEstlddkDIDECIKKIKELKNH 1430
Ank_2 pfam12796
Ankyrin repeats (3 copies);
879-930 3.81e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392922079   879 LLDAVREiNKTNAVNA-VKAGSYINAFNKFGNTALHTATKSALPEIVKLLIKN 930
Cdd:pfam12796    1 LHLAAKN-GNLELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 1006-1062 8.40e-03

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 36.19  E-value: 8.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392922079 1006 QFMEKFQAITSDEANSNTTHVIVKTDENgaletdSLDLLLWVFNGAIIVKEQWMVDC 1062
Cdd:cd00027    18 KLIEALGGKVSESLSSKVTHLIAKSPSG------EKYYLAALAWGIPIVSPEWLLDC 68
 
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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