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Conserved domains on  [gi|19115033|ref|NP_594121|]
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CHS5-like protein Cfr1 [Schizosaccharomyces pombe]

Protein Classification

BRCT domain-containing protein( domain architecture ID 10883201)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fn3_2 pfam16893
Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin ...
 78-166 3.55e-50

Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin biosynthesis protein CHS5 where, together with the neighbouring BRCT domain (pfam00533), it binds to the Arf1 GTPase.


:

Pssm-ID: 435634  Cd Length: 89  Bit Score: 168.53  E-value: 3.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033    78 KLPSPPVLKLKNATQTSIVLEWDPLQLSTARLKSLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLVLDTTAGTF 157
Cdd:pfam16893   1 NSPKAPVLKVRNVTQTSVVLEWDPLELGTAKLKSLDLYRNGQRLGVIPNPLTNTSTKLSGLSVDTEYTFQLVLRTTAGTY 80


                  ....*....
gi 19115033   158 PSKHITIKT 166
Cdd:pfam16893  81 WSNKIKVRT 89
Chs5_N cd13945
N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex ...
 5-77 3.37e-33

N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex conserved in fungi that interacts with chitin synthase III (Chs3p) and is involved in its transport to the cell surface from the trans-Golgi network, functioning as an exomer cargo adapter. Chs5p appears to form a complex with Chs6p and its paralogs Bch1p, Bud7p, and Bch2p. In this complex, Chs5p may act as a central scaffold. The N-terminal domain characterized by this model forms a homodimer and has been shown to interact with Chs6p and Bch1p. It may function as a flexible hinge domain that allows the exomer to interact with both proteins and the Golgi membrane as the latter undergoes changes in curvature during the formation of transport vesicles. The dimerization domain sits N-terminally to a conserved FBE (FN3-BRCT) unit, which binds Arf1 an is involved in the recruitment of the exomer to the membrane.


:

Pssm-ID: 260117  Cd Length: 73  Bit Score: 121.52  E-value: 3.37e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115033   5 NQFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHNKEEEIARETAFDDVQKEIFETYGQ 77
Cdd:cd13945   1 VEVSLTVGKLDAGLAILLTSDHHLIEFPSVLLPPGIKAGSIVKITVSRNLEAEKKEEEEFQSLQKEILETYGT 73
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 173-249 2.38e-23

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.


The actual alignment was detected with superfamily member cd17742:

Pssm-ID: 469589 [Multi-domain]  Cd Length: 77  Bit Score: 93.94  E-value: 2.38e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115033 173 TGIQVCVGNMVPNE-MEALQKCIERIHARPIQtSVRIDTTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLV 249
Cdd:cd17742   1 SGITVCLGPLDPPEsVDELEQCLERIGAKPTD-RVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLRACEVEKKIV 77
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
270-376 5.11e-04

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  270 SVEAAQNAAPNLNATTEQPKNTAEV-----AQGAASAKAPQQTTQQGTqnSANAEPSSSASVPAEAPETEAEQSIDVSSD 344
Cdd:PRK13108 345 AAESVVQVADRDGESTPAVEETSEAdiereQPGDLAGQAPAAHQVDAE--AASAAPEEPAALASEAHDETEPEVPEKAAP 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19115033  345 IglrSDSSKPNE--------APTSSENIKADQPENSTKQE 376
Cdd:PRK13108 423 I---PDPAKPDElavagpgdDPAEPDGIRRQDDFSSRRRR 459
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 324-468 4.39e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  324 ASVPAEAPETEAEQSiDVSSDIGLRSDSSKPNEAPtSSENIKADQPENSTKQENPEedmqikdaeehSNLESTPAAQQTS 403
Cdd:NF033609  33 SSKEADASENSVTQS-DSASNESKSNDSSSVSAAP-KTDDTNVSDTKTSSNTNNGE-----------TSVAQNPAQQETT 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033  404 EVEANNHQEKPSSLPAVEQINVNEENNTPETegledeKEENNTAAESLINQ--EETTSGEAVTKSTV 468
Cdd:NF033609 100 QSASTNATTEETPVTGEATTTATNQANTPAT------TQSSNTNAEELVNQtsNETTSNDTNTVSSV 160
 
Name Accession Description Interval E-value
fn3_2 pfam16893
Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin ...
 78-166 3.55e-50

Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin biosynthesis protein CHS5 where, together with the neighbouring BRCT domain (pfam00533), it binds to the Arf1 GTPase.


Pssm-ID: 435634  Cd Length: 89  Bit Score: 168.53  E-value: 3.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033    78 KLPSPPVLKLKNATQTSIVLEWDPLQLSTARLKSLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLVLDTTAGTF 157
Cdd:pfam16893   1 NSPKAPVLKVRNVTQTSVVLEWDPLELGTAKLKSLDLYRNGQRLGVIPNPLTNTSTKLSGLSVDTEYTFQLVLRTTAGTY 80


                  ....*....
gi 19115033   158 PSKHITIKT 166
Cdd:pfam16893  81 WSNKIKVRT 89
Chs5_N cd13945
N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex ...
 5-77 3.37e-33

N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex conserved in fungi that interacts with chitin synthase III (Chs3p) and is involved in its transport to the cell surface from the trans-Golgi network, functioning as an exomer cargo adapter. Chs5p appears to form a complex with Chs6p and its paralogs Bch1p, Bud7p, and Bch2p. In this complex, Chs5p may act as a central scaffold. The N-terminal domain characterized by this model forms a homodimer and has been shown to interact with Chs6p and Bch1p. It may function as a flexible hinge domain that allows the exomer to interact with both proteins and the Golgi membrane as the latter undergoes changes in curvature during the formation of transport vesicles. The dimerization domain sits N-terminally to a conserved FBE (FN3-BRCT) unit, which binds Arf1 an is involved in the recruitment of the exomer to the membrane.


Pssm-ID: 260117  Cd Length: 73  Bit Score: 121.52  E-value: 3.37e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115033   5 NQFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHNKEEEIARETAFDDVQKEIFETYGQ 77
Cdd:cd13945   1 VEVSLTVGKLDAGLAILLTSDHHLIEFPSVLLPPGIKAGSIVKITVSRNLEAEKKEEEEFQSLQKEILETYGT 73
CHS5_N pfam16892
Chitin biosynthesis protein CHS5 N-terminus; This domain is found at the N-terminus of fungal ...
 6-53 1.93e-23

Chitin biosynthesis protein CHS5 N-terminus; This domain is found at the N-terminus of fungal chitin biosynthesis protein CHS5. It functions as a dimerization domain.


Pssm-ID: 407128  Cd Length: 48  Bit Score: 93.11  E-value: 1.93e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 19115033     6 QFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHN 53
Cdd:pfam16892   1 EVTFTVGKLDAGMAILLTSDHHLIEFPSVLLPPGVTAGSIVDISVSRN 48
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 173-249 2.38e-23

BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth.


Pssm-ID: 349373 [Multi-domain]  Cd Length: 77  Bit Score: 93.94  E-value: 2.38e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115033 173 TGIQVCVGNMVPNE-MEALQKCIERIHARPIQtSVRIDTTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLV 249
Cdd:cd17742   1 SGITVCLGPLDPPEsVDELEQCLERIGAKPTD-RVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLRACEVEKKIV 77
BRCT smart00292
breast cancer carboxy-terminal domain;
169-242 1.13e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.07  E-value: 1.13e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033    169 MIDLTGIQVCV-GNMVPNEMEALQKCIERIHARPIQTSVRIDTTHFICSSTGGPEYE--KAKAANIPILGLDYLLKC 242
Cdd:smart00292   1 PKLFKGKTFYItGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDC 77
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 177-237 1.80e-07

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 48.35  E-value: 1.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115033   177 VCVGNMVPNEMEALQKCIERIHARpIQTSVRIDTTHFICSSTGGPEYEKAKAANIPILGLD 237
Cdd:pfam12738   3 ICVTGFDGDDREGLQKLIEAMGAE-YTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPL 62
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 80-166 1.87e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  80 PSPPV-LKLKNATQTSIVLEWDPLQLSTARLKS-LCLYR----NNVRVLNiSNPMTTHNAKLSGLSLDTEYDFSLVLDTT 153
Cdd:cd00063   1 PSPPTnLRVTDVTSTSVTLSWTPPEDDGGPITGyVVEYRekgsGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                        90
                ....*....|....
gi 19115033 154 AGT-FPSKHITIKT 166
Cdd:cd00063  80 GGEsPPSESVTVTT 93
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 270-376 5.11e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  270 SVEAAQNAAPNLNATTEQPKNTAEV-----AQGAASAKAPQQTTQQGTqnSANAEPSSSASVPAEAPETEAEQSIDVSSD 344
Cdd:PRK13108 345 AAESVVQVADRDGESTPAVEETSEAdiereQPGDLAGQAPAAHQVDAE--AASAAPEEPAALASEAHDETEPEVPEKAAP 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19115033  345 IglrSDSSKPNE--------APTSSENIKADQPENSTKQE 376
Cdd:PRK13108 423 I---PDPAKPDElavagpgdDPAEPDGIRRQDDFSSRRRR 459
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 80-149 2.55e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.21  E-value: 2.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115033     80 PSPPV-LKLKNATQTSIVLEWDPLQLSTARLK----SLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLV 149
Cdd:smart00060   1 PSPPSnLRVTDVTSTSVTLSWEPPPDDGITGYivgyRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 324-468 4.39e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  324 ASVPAEAPETEAEQSiDVSSDIGLRSDSSKPNEAPtSSENIKADQPENSTKQENPEedmqikdaeehSNLESTPAAQQTS 403
Cdd:NF033609  33 SSKEADASENSVTQS-DSASNESKSNDSSSVSAAP-KTDDTNVSDTKTSSNTNNGE-----------TSVAQNPAQQETT 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033  404 EVEANNHQEKPSSLPAVEQINVNEENNTPETegledeKEENNTAAESLINQ--EETTSGEAVTKSTV 468
Cdd:NF033609 100 QSASTNATTEETPVTGEATTTATNQANTPAT------TQSSNTNAEELVNQtsNETTSNDTNTVSSV 160
 
Name Accession Description Interval E-value
fn3_2 pfam16893
Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin ...
 78-166 3.55e-50

Fibronectin type III domain; This fibronectin type III domain is found in fungal chitin biosynthesis protein CHS5 where, together with the neighbouring BRCT domain (pfam00533), it binds to the Arf1 GTPase.


Pssm-ID: 435634  Cd Length: 89  Bit Score: 168.53  E-value: 3.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033    78 KLPSPPVLKLKNATQTSIVLEWDPLQLSTARLKSLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLVLDTTAGTF 157
Cdd:pfam16893   1 NSPKAPVLKVRNVTQTSVVLEWDPLELGTAKLKSLDLYRNGQRLGVIPNPLTNTSTKLSGLSVDTEYTFQLVLRTTAGTY 80


                  ....*....
gi 19115033   158 PSKHITIKT 166
Cdd:pfam16893  81 WSNKIKVRT 89
Chs5_N cd13945
N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex ...
 5-77 3.37e-33

N-terminal dimerization domain of Chs5 and similar proteins; Chs5/6 is a multi-protein complex conserved in fungi that interacts with chitin synthase III (Chs3p) and is involved in its transport to the cell surface from the trans-Golgi network, functioning as an exomer cargo adapter. Chs5p appears to form a complex with Chs6p and its paralogs Bch1p, Bud7p, and Bch2p. In this complex, Chs5p may act as a central scaffold. The N-terminal domain characterized by this model forms a homodimer and has been shown to interact with Chs6p and Bch1p. It may function as a flexible hinge domain that allows the exomer to interact with both proteins and the Golgi membrane as the latter undergoes changes in curvature during the formation of transport vesicles. The dimerization domain sits N-terminally to a conserved FBE (FN3-BRCT) unit, which binds Arf1 an is involved in the recruitment of the exomer to the membrane.


Pssm-ID: 260117  Cd Length: 73  Bit Score: 121.52  E-value: 3.37e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115033   5 NQFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHNKEEEIARETAFDDVQKEIFETYGQ 77
Cdd:cd13945   1 VEVSLTVGKLDAGLAILLTSDHHLIEFPSVLLPPGIKAGSIVKITVSRNLEAEKKEEEEFQSLQKEILETYGT 73
CHS5_N pfam16892
Chitin biosynthesis protein CHS5 N-terminus; This domain is found at the N-terminus of fungal ...
 6-53 1.93e-23

Chitin biosynthesis protein CHS5 N-terminus; This domain is found at the N-terminus of fungal chitin biosynthesis protein CHS5. It functions as a dimerization domain.


Pssm-ID: 407128  Cd Length: 48  Bit Score: 93.11  E-value: 1.93e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 19115033     6 QFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHN 53
Cdd:pfam16892   1 EVTFTVGKLDAGMAILLTSDHHLIEFPSVLLPPGVTAGSIVDISVSRN 48
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 173-249 2.38e-23

BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth.


Pssm-ID: 349373 [Multi-domain]  Cd Length: 77  Bit Score: 93.94  E-value: 2.38e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115033 173 TGIQVCVGNMVPNE-MEALQKCIERIHARPIQtSVRIDTTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLV 249
Cdd:cd17742   1 SGITVCLGPLDPPEsVDELEQCLERIGAKPTD-RVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLRACEVEKKIV 77
BRCT smart00292
breast cancer carboxy-terminal domain;
169-242 1.13e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.07  E-value: 1.13e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033    169 MIDLTGIQVCV-GNMVPNEMEALQKCIERIHARPIQTSVRIDTTHFICSSTGGPEYE--KAKAANIPILGLDYLLKC 242
Cdd:smart00292   1 PKLFKGKTFYItGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDC 77
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 177-242 5.09e-08

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: 50.05  E-value: 5.09e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033 177 VCVGNMVPNEMEALQKCIERIHARpIQTSVRIDTTHFICSSTGGPEY-EKAKAANIPILGLDYLLKC 242
Cdd:cd00027   3 ICFSGLDDEEREELKKLIEALGGK-VSESLSSKVTHLIAKSPSGEKYyLAALAWGIPIVSPEWLLDC 68
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 177-237 1.80e-07

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 48.35  E-value: 1.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115033   177 VCVGNMVPNEMEALQKCIERIHARpIQTSVRIDTTHFICSSTGGPEYEKAKAANIPILGLD 237
Cdd:pfam12738   3 ICVTGFDGDDREGLQKLIEAMGAE-YTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPL 62
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 168-242 2.80e-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: 45.36  E-value: 2.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115033   168 RMIDLTGIQVCVGNMVPNEMEALQKCIERIHARpIQTSVRIDTTHFICSStGGPEYEKAKAANIPILGLDYLLKC 242
Cdd:pfam00533   2 KEKLFSGKTFVITGLDGLERDELKELIEKLGGK-VTDSLSKKTTHVIVEA-RTKKYLKAKELGIPIVTEEWLLDC 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 80-166 1.87e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  80 PSPPV-LKLKNATQTSIVLEWDPLQLSTARLKS-LCLYR----NNVRVLNiSNPMTTHNAKLSGLSLDTEYDFSLVLDTT 153
Cdd:cd00063   1 PSPPTnLRVTDVTSTSVTLSWTPPEDDGGPITGyVVEYRekgsGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                        90
                ....*....|....
gi 19115033 154 AGT-FPSKHITIKT 166
Cdd:cd00063  80 GGEsPPSESVTVTT 93
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 270-376 5.11e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  270 SVEAAQNAAPNLNATTEQPKNTAEV-----AQGAASAKAPQQTTQQGTqnSANAEPSSSASVPAEAPETEAEQSIDVSSD 344
Cdd:PRK13108 345 AAESVVQVADRDGESTPAVEETSEAdiereQPGDLAGQAPAAHQVDAE--AASAAPEEPAALASEAHDETEPEVPEKAAP 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19115033  345 IglrSDSSKPNE--------APTSSENIKADQPENSTKQE 376
Cdd:PRK13108 423 I---PDPAKPDElavagpgdDPAEPDGIRRQDDFSSRRRR 459
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
259-419 1.42e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.76  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  259 RASYNANASINSVEAAQNAAPNLNATTEQPKNTAEVAQGAASAKAPQQTTQQGTqnsANAEPSSSASVPAEAPETEAEQS 338
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPA---TADRGDDAADGDAPVPAKANARA 457

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  339 IDVSSDIglrSDSSKPNEAPTSSENIKADQPENSTKQENPEEDMQIKDAEEHSNLESTPAAQQTSEVEANNHQEKPSSLP 418
Cdd:PRK07003 458 SADSRCD---ERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARP 534


                 .
gi 19115033  419 A 419
Cdd:PRK07003 535 P 535
BRCT_BRC1_like_rpt4 cd18438
fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 209-242 1.68e-03

fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat.


Pssm-ID: 349391 [Multi-domain]  Cd Length: 68  Bit Score: 37.36  E-value: 1.68e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 19115033 209 DTTHFICSSTGGPEYEKAKAANIPILGLDYLLKC 242
Cdd:cd18438  34 DNTHLITASPEGEKYEAAKEWNIPIVNHLWLYDS 67
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 80-149 2.55e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.21  E-value: 2.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115033     80 PSPPV-LKLKNATQTSIVLEWDPLQLSTARLK----SLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLV 149
Cdd:smart00060   1 PSPPSnLRVTDVTSTSVTLSWEPPPDDGITGYivgyRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75
BRCT_TopBP1_rpt5 cd18434
fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 210-249 2.87e-03

fifth 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 fifth BRCT domain.


Pssm-ID: 349387  Cd Length: 89  Bit Score: 37.28  E-value: 2.87e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 19115033 210 TTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLV 249
Cdd:cd18434  48 STHLVLKEPEGSKYEAAKKWNLPAVTKSWLFECARTGKKV 87
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 172-250 3.15e-03

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 36.88  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033 172 LTGIQVCV---GNMVPNEMEALQKCIERiHARPIQTSVRIDTTHFICSSTGGPEYEKAKAA---NIPILGLDYLLKCESE 245
Cdd:cd17726   2 FSGCQIVLdlkTLPGFKEKKKLKKKITE-NGGIISYIINKKCTHVVVNNAKALSSYKCRMAqkyGIPVVSLDYIWKCVEA 80


                ....*
gi 19115033 246 GRLVN 250
Cdd:cd17726  81 GKLLD 85
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 172-242 3.66e-03

second 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 second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 36.75  E-value: 3.66e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115033 172 LTGIQVCVGNMVPNEMEALQKCIER---IHARpiqtSVRIDTTHFICSSTGGPEYEKAKAAN-IPILGLDYLLKC 242
Cdd:cd17731   3 FKGLVICVTGFDSEERKEIQQLVEQnggSYSP----DLSKNCTHLIAGSPSGQKYEFARKWNsIHIVTPEWLYDS 73
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 324-468 4.39e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  324 ASVPAEAPETEAEQSiDVSSDIGLRSDSSKPNEAPtSSENIKADQPENSTKQENPEedmqikdaeehSNLESTPAAQQTS 403
Cdd:NF033609  33 SSKEADASENSVTQS-DSASNESKSNDSSSVSAAP-KTDDTNVSDTKTSSNTNNGE-----------TSVAQNPAQQETT 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115033  404 EVEANNHQEKPSSLPAVEQINVNEENNTPETegledeKEENNTAAESLINQ--EETTSGEAVTKSTV 468
Cdd:NF033609 100 QSASTNATTEETPVTGEATTTATNQANTPAT------TQSSNTNAEELVNQtsNETTSNDTNTVSSV 160
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 264-416 4.41e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.96  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115033  264 ANASINSVEAAQNAAPNLNATTEQPKNTAEVAQGAASAKAPQQTTQQGTQNSANAEPSSSASVPAEAPETEAEQSIDVSS 343
Cdd:PRK13108 302 ELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAG 381

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115033  344 DIGL--RSDSSKPNEAPTSSENIKADQPENSTKQEnPEEDMQIKDAEEHSNLESTPAAQQTSEVEANNHQEKPSS 416
Cdd:PRK13108 382 QAPAahQVDAEAASAAPEEPAALASEAHDETEPEV-PEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSS 455
 
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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