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Conserved domains on  [gi|58866050|ref|NP_067520|]
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baculoviral IAP repeat-containing protein 1g [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
 767-873 4.74e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


:

Pssm-ID: 436120  Cd Length: 106  Bit Score: 169.39  E-value: 4.74e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 58866050    847 GLWLVSPESFSSFVSEHLLRLALIFAY 873
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 464-618 1.71e-39

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 144.37  E-value: 1.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    464 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLDNIICTQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLFRTCLLIAVHTNRVRDIRPYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 58866050    609 FVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.96e-31

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


:

Pssm-ID: 459891  Cd Length: 68  Bit Score: 117.76  E-value: 1.96e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    162 RLESFEDWPFYAHGT-SPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQ 228
Cdd:pfam00653    1 RLATFENWPHSNKSPpTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 279-346 3.28e-28

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


:

Pssm-ID: 237989  Cd Length: 69  Bit Score: 108.51  E-value: 3.28e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050  279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 63-128 2.15e-24

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


:

Pssm-ID: 459891  Cd Length: 68  Bit Score: 97.73  E-value: 2.15e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050     63 RLKTFESY--DTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 128
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 688-743 4.69e-06

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 45.25  E-value: 4.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDvKLTTFLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
1076-1240 5.84e-06

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1076 LPALQSLEVSETN--QLPDQLFhNLHKflgLKELCVRLDGkpdvLSVLPEEFLNLHHMEKLSIrtsTESDLSKLVKFIQN 1153
Cdd:COG4886  135 LTNLKELDLSNNQltDLPEPLG-NLTN---LKSLDLSNNQ----LTDLPEELGNLTNLKELDL---SNNQITDLPEPLGN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1154 FPNLHVFHLKCDFLSnceSLMTALASCKKLREIEFSGQCFEAMTFvniLPNFVSLKILSLKGQQFADKETsekfaqaLGS 1233
Cdd:COG4886  204 LTNLEELDLSGNQLT---DLPEPLANLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDLPP-------LAN 270


                 ....*..
gi 58866050 1234 LRNLEEL 1240
Cdd:COG4886  271 LTNLKTL 277
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
 767-873 4.74e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 169.39  E-value: 4.74e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 58866050    847 GLWLVSPESFSSFVSEHLLRLALIFAY 873
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 464-618 1.71e-39

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 144.37  E-value: 1.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    464 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLDNIICTQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLFRTCLLIAVHTNRVRDIRPYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 58866050    609 FVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.96e-31

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 117.76  E-value: 1.96e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    162 RLESFEDWPFYAHGT-SPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQ 228
Cdd:pfam00653    1 RLATFENWPHSNKSPpTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 159-229 2.02e-31

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 117.80  E-value: 2.02e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58866050     159 EEARLESFEDWPFYAHgTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:smart00238    2 EEARLKTFQNWPYNSK-CTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 160-229 6.47e-30

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 113.51  E-value: 6.47e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  160 EARLESFEDWPfYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:cd00022    1 EARLKTFKNWP-ISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 279-346 3.28e-28

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 108.51  E-value: 3.28e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050  279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 277-346 4.36e-28

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 108.17  E-value: 4.36e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050     277 NEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 281-346 5.59e-27

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 105.05  E-value: 5.59e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    281 RMDMFKDWP--QESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:pfam00653    1 RLATFENWPhsNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 63-128 2.15e-24

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 97.73  E-value: 2.15e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050     63 RLKTFESY--DTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 128
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 61-129 1.01e-22

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 92.71  E-value: 1.01e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58866050   61 AKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 59-129 1.10e-19

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 84.29  E-value: 1.10e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58866050      59 SEAKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
450-918 1.58e-18

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 92.18  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  450 QGALTIPEVFSNLSSVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPDQGLDNIICTQLLGAGGC 529
Cdd:COG5635  167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  530 ISEvclssSIQQL--QHQVLFLLDDY------SGLASLPQALHTLITKNYlfRTCLLIAVHTNRVRDIRPYLGTSLEIQE 601
Cdd:COG5635  245 PED-----ALERLlrNGRLLLLLDGLdevpdeADRDEVLNQLRRFLERYP--KARVIITSRPEGYDSSELEGFEVLELAP 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  602 FPFYNTVFVLRKFFSHDIICVEKLIIYFSENKDLQGVYKTPLFVAAVCNDWNQNASAQDDfqDVTLFHSYMQYLsLKYKA 681
Cdd:COG5635  318 LSDEQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDT--RAELYEQFVELL-LERWD 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  682 TAESLQATVSS--------CGQLALTGLFSSCFEFNSDDLAEAgvdedvkLTTFLMSKFTAQRL---------------R 738
Cdd:COG5635  395 EQRGLTIYRELsreelrelLSELALAMQENGRTEFAREELEEI-------LREYLGRRKDAEALldelllrtgllvergE 467

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  739 PVYRFLGPLFQEFLAAVRLTELLSSDRQEdqdlglyylrQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLqlvDE 818
Cdd:COG5635  468 GRYSFAHRSFQEYLAARALVEELDEELLE----------LLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALL---AR 534

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  819 KESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESFSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGRTLALRV 898
Cdd:COG5635  535 DDAAALALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLL 614

                        490       500
                 ....*....|....*....|
gi 58866050  899 LNLEYFWDHPESLLLLRSLK 918
Cdd:COG5635  615 LLALALLLALLLLLLLLLLA 634
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 688-743 4.69e-06

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 45.25  E-value: 4.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDvKLTTFLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1076-1240 5.84e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1076 LPALQSLEVSETN--QLPDQLFhNLHKflgLKELCVRLDGkpdvLSVLPEEFLNLHHMEKLSIrtsTESDLSKLVKFIQN 1153
Cdd:COG4886  135 LTNLKELDLSNNQltDLPEPLG-NLTN---LKSLDLSNNQ----LTDLPEELGNLTNLKELDL---SNNQITDLPEPLGN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1154 FPNLHVFHLKCDFLSnceSLMTALASCKKLREIEFSGQCFEAMTFvniLPNFVSLKILSLKGQQFADKETsekfaqaLGS 1233
Cdd:COG4886  204 LTNLEELDLSGNQLT---DLPEPLANLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDLPP-------LAN 270


                 ....*..
gi 58866050 1234 LRNLEEL 1240
Cdd:COG4886  271 LTNLKTL 277
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1072-1271 8.03e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 45.78  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1072 LLLTLPALQSLEVSETNQLPDQLFHNLHKfLGLKElCVRLDGKPDVLSvlpeeflNLHHMEKLSIRTSTESDLSKLVKFI 1151
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1152 QNFPNLHVFHLK-CDFLSNceSLMTALA-SCKKLREIEF----SGQCFEAMTFVNILPNFVSLKILSLKGQQFADKETse 1225
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD--SGIVALAtNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGV-- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58866050 1226 kFAQALGSLRNLEELLVP-----TGDGIHQVakLIVRQClqlPCLRVLAFH 1271
Cdd:cd09293  151 -WELASGCSKSLERLSLNncrnlTDQSIPAI--LASNYF---PNLSVLEFR 195
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 445-570 4.22e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 42.70  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  445 ISQPVQGALTIPEVFSNLSSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSITpDQGLDNI 518
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  519 ICTQLLG--AGGCISEVCLSSSIQQLQHQVLFLLD------DYSGLASLPQALHTLITKN 570
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDepstglHQQDINQLLEVIKGLIDLG 139
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
 767-873 4.74e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 169.39  E-value: 4.74e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 58866050    847 GLWLVSPESFSSFVSEHLLRLALIFAY 873
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 464-618 1.71e-39

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 144.37  E-value: 1.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    464 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLDNIICTQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050    541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLFRTCLLIAVHTNRVRDIRPYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 58866050    609 FVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.96e-31

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 117.76  E-value: 1.96e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    162 RLESFEDWPFYAHGT-SPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQ 228
Cdd:pfam00653    1 RLATFENWPHSNKSPpTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 159-229 2.02e-31

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 117.80  E-value: 2.02e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58866050     159 EEARLESFEDWPFYAHgTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:smart00238    2 EEARLKTFQNWPYNSK-CTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 160-229 6.47e-30

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 113.51  E-value: 6.47e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  160 EARLESFEDWPfYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:cd00022    1 EARLKTFKNWP-ISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 279-346 3.28e-28

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 108.51  E-value: 3.28e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050  279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 277-346 4.36e-28

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 108.17  E-value: 4.36e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050     277 NEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 281-346 5.59e-27

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 105.05  E-value: 5.59e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    281 RMDMFKDWP--QESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:pfam00653    1 RLATFENWPhsNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 63-128 2.15e-24

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 97.73  E-value: 2.15e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050     63 RLKTFESY--DTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 128
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 61-129 1.01e-22

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 92.71  E-value: 1.01e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58866050   61 AKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 59-129 1.10e-19

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 84.29  E-value: 1.10e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58866050      59 SEAKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
450-918 1.58e-18

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 92.18  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  450 QGALTIPEVFSNLSSVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPDQGLDNIICTQLLGAGGC 529
Cdd:COG5635  167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  530 ISEvclssSIQQL--QHQVLFLLDDY------SGLASLPQALHTLITKNYlfRTCLLIAVHTNRVRDIRPYLGTSLEIQE 601
Cdd:COG5635  245 PED-----ALERLlrNGRLLLLLDGLdevpdeADRDEVLNQLRRFLERYP--KARVIITSRPEGYDSSELEGFEVLELAP 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  602 FPFYNTVFVLRKFFSHDIICVEKLIIYFSENKDLQGVYKTPLFVAAVCNDWNQNASAQDDfqDVTLFHSYMQYLsLKYKA 681
Cdd:COG5635  318 LSDEQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDT--RAELYEQFVELL-LERWD 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  682 TAESLQATVSS--------CGQLALTGLFSSCFEFNSDDLAEAgvdedvkLTTFLMSKFTAQRL---------------R 738
Cdd:COG5635  395 EQRGLTIYRELsreelrelLSELALAMQENGRTEFAREELEEI-------LREYLGRRKDAEALldelllrtgllvergE 467

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  739 PVYRFLGPLFQEFLAAVRLTELLSSDRQEdqdlglyylrQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLqlvDE 818
Cdd:COG5635  468 GRYSFAHRSFQEYLAARALVEELDEELLE----------LLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALL---AR 534

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  819 KESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESFSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGRTLALRV 898
Cdd:COG5635  535 DDAAALALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLL 614

                        490       500
                 ....*....|....*....|
gi 58866050  899 LNLEYFWDHPESLLLLRSLK 918
Cdd:COG5635  615 LLALALLLALLLLLLLLLLA 634
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 688-743 4.69e-06

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 45.25  E-value: 4.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050    688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDvKLTTFLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1076-1240 5.84e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1076 LPALQSLEVSETN--QLPDQLFhNLHKflgLKELCVRLDGkpdvLSVLPEEFLNLHHMEKLSIrtsTESDLSKLVKFIQN 1153
Cdd:COG4886  135 LTNLKELDLSNNQltDLPEPLG-NLTN---LKSLDLSNNQ----LTDLPEELGNLTNLKELDL---SNNQITDLPEPLGN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1154 FPNLHVFHLKCDFLSnceSLMTALASCKKLREIEFSGQCFEAMTFvniLPNFVSLKILSLKGQQFADKETsekfaqaLGS 1233
Cdd:COG4886  204 LTNLEELDLSGNQLT---DLPEPLANLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDLPP-------LAN 270


                 ....*..
gi 58866050 1234 LRNLEEL 1240
Cdd:COG4886  271 LTNLKTL 277
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1118-1335 1.13e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.55  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1118 LSVLPEEFLNLHHMEKLSIRtstESDLSKLVKFIQNFPNLHVFHLKCDFLSnceSLMTALASCKKLREIEFSGQCFEAMT 1197
Cdd:COG4886  125 LTDLPEELANLTNLKELDLS---NNQLTDLPEPLGNLTNLKSLDLSNNQLT---DLPEELGNLTNLKELDLSNNQITDLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1198 FVniLPNFVSLKILSLKGQQFADketsekFAQALGSLRNLEELLVpTGDGIHQVAKLivrqcLQLPCLRVLAfhdiLDDE 1277
Cdd:COG4886  199 EP--LGNLTNLEELDLSGNQLTD------LPEPLANLTNLETLDL-SNNQLTDLPEL-----GNLTNLEELD----LSNN 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050 1278 SVIEIGaaTSGSFQKLENLDISMNhKITEEGYRNFFQALDNLPNLQMLNICRNIPGRI 1335
Cdd:COG4886  261 QLTDLP--PLANLTNLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1072-1271 8.03e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 45.78  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1072 LLLTLPALQSLEVSETNQLPDQLFHNLHKfLGLKElCVRLDGKPDVLSvlpeeflNLHHMEKLSIRTSTESDLSKLVKFI 1151
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1152 QNFPNLHVFHLK-CDFLSNceSLMTALA-SCKKLREIEF----SGQCFEAMTFVNILPNFVSLKILSLKGQQFADKETse 1225
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD--SGIVALAtNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGV-- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58866050 1226 kFAQALGSLRNLEELLVP-----TGDGIHQVakLIVRQClqlPCLRVLAFH 1271
Cdd:cd09293  151 -WELASGCSKSLERLSLNncrnlTDQSIPAI--LASNYF---PNLSVLEFR 195
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1134-1364 2.78e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.92  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1134 LSIRTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMTALASCKKLREIEFSGQcfeamtfvNILPNFVSLKILSL 1213
Cdd:COG4886   49 LTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN--------EELSNLTNLESLDL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1214 KGQQFADketsekFAQALGSLRNLEELLVpTGDGIHQVAKLIVrqclQLPCLRVLAfhdiLDDESVIEIGAAtSGSFQKL 1293
Cdd:COG4886  121 SGNQLTD------LPEELANLTNLKELDL-SNNQLTDLPEPLG----NLTNLKSLD----LSNNQLTDLPEE-LGNLTNL 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58866050 1294 ENLDISMNhKITEegyrnFFQALDNLPNLQMLNICRN----IPGRIQvQATTVKALC--HC-VSRLPSLTRLGMLSWL 1364
Cdd:COG4886  185 KELDLSNN-QITD-----LPEPLGNLTNLEELDLSGNqltdLPEPLA-NLTNLETLDlsNNqLTDLPELGNLTNLEEL 255
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 445-570 4.22e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 42.70  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  445 ISQPVQGALTIPEVFSNLSSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSITpDQGLDNI 518
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050  519 ICTQLLG--AGGCISEVCLSSSIQQLQHQVLFLLD------DYSGLASLPQALHTLITKN 570
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDepstglHQQDINQLLEVIKGLIDLG 139
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1107-1370 1.09e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 42.73  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1107 LCVRLDGKPDVLSVLPEEFLNLHHMEKLSIR--TSTESDLSKLVKFIQNFPNLHVFHLKCDFL----SNCESLMTALASC 1180
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEgnTLGEEAAKALASALRPQPSLKELCLSLNETgripRGLQSLLQGLTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1181 KKLREIEFS--GQCFEAMTFVNILPNFVSLKILSLKGQQFADkeTSEKF-AQALGSLRnleellvptgdgiHQVAKLIVR 1257
Cdd:cd00116   81 CGLQELDLSdnALGPDGCGVLESLLRSSSLQELKLNNNGLGD--RGLRLlAKGLKDLP-------------PALEKLVLG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1258 QCLqlpclrvlafhdiLDDESVIEIGAATSgSFQKLENLDISMNHkITEEGYRNFFQALDNLPNLQMLNICRNipgriQV 1337
Cdd:cd00116  146 RNR-------------LEGASCEALAKALR-ANRDLKELNLANNG-IGDAGIRALAEGLKANCNLEVLDLNNN-----GL 205

                        250       260       270
                 ....*....|....*....|....*....|...
gi 58866050 1338 QATTVKALCHCVSRLPSLTRLGMLSWLLDEEDM 1370
Cdd:cd00116  206 TDEGASALAETLASLKSLEVLNLGDNNLTDAGA 238
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1058-1379 2.32e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.08  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1058 CSMSRLELsrAEQELLLTLPALQsLEVSETNQLPD--QLFHNLHKFLGLKELCVRLDGKPDVLSVL---PEEFLNLHHME 1132
Cdd:COG5238   98 EEVSPVAL--AETATAVATPPPD-LRRIMAKTLEDslILYLALPRRINLIQVLKDPLGGNAVHLLGlaaRLGLLAAISMA 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1133 KLSIRTSTES-DLS----------KLVKFIQNFPNLHVFHLKCDFL--SNCESLMTALASCKKLREIEFSGQCF---EAM 1196
Cdd:COG5238  175 KALQNNSVETvYLGcnqigdegieELAEALTQNTTVTTLWLKRNPIgdEGAEILAEALKGNKSLTTLDLSNNQIgdeGVI 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1197 TFVNILPNFVSLKILSLKGQQFaDKETSEKFAQALGSLRNLEELLV---PTGD-GIHQVAK-LIVRQCLQLPCLRvlafH 1271
Cdd:COG5238  255 ALAEALKNNTTVETLYLSGNQI-GAEGAIALAKALQGNTTLTSLDLsvnRIGDeGAIALAEgLQGNKTLHTLNLA----Y 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866050 1272 DILDDESVIEIGAATSGSfQKLENLDISMNhKITEEGYRNFFQALDNLPNLQMLNICRNIPGRIQVQAtTVKALCHcvsr 1351
Cdd:COG5238  330 NGIGAQGAIALAKALQEN-TTLHSLDLSDN-QIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEA-LIDALQT---- 402

                        330       340
                 ....*....|....*....|....*...
gi 58866050 1352 lPSLTRLGMLSWLLDEEDMKVINDVKER 1379
Cdd:COG5238  403 -NRLHTLILDGNLIGAEAQQRLEQLLER 429
 
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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