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Conserved domains on  [gi|5932012|gb|AAD56764|]
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neuronal apoptosis inhibitory protein [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 5.87e-41

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: 146.27  E-value: 5.87e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 5932012     847 GLWLVSPESSSSFVSEHLLRLALIFAY 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 6.01e-40

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: 145.91  E-value: 6.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     464 SVMCVEGETGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 5932012     609 SVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.09e-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: 118.53  E-value: 1.09e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     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 2.14e-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: 108.89  E-value: 2.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012   279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 63-128 8.80e-25

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: 98.89  E-value: 8.80e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012      63 RLKTFETY--DTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 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 5.03e-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: 44.86  E-value: 5.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDeKLTTLLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1072-1271 1.30e-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.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.09  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1072 LLLTLPALQSLEVSETNQLPEQLFHNLHKfLGLKElCVRLDGKPDVLSvlpgefpNLHHMEKLSIRTSTESDLSKLVKFI 1151
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1152 QNFPNLHVFHLK-CDFLSNcESLMAVLASCKKLREIEFsGRCFEAmtfvnILPNFVSLKIL-----NLKDQQFPDKETSE 1225
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD-SGIVALATNCPKLQTINL-GRHRNG-----HLITDVSLSALgknctFLQTVGFAGCDVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5932012  1226 KFAQALGSLR--NLEELLVP-----TGDGIHQVakLIVRQClqlPCLRVLTFH 1271
Cdd:cd09293  148 KGVWELASGCskSLERLSLNncrnlTDQSIPAI--LASNYF---PNLSVLEFR 195
 
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 5.87e-41

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: 146.27  E-value: 5.87e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 5932012     847 GLWLVSPESSSSFVSEHLLRLALIFAY 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 6.01e-40

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: 145.91  E-value: 6.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     464 SVMCVEGETGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 5932012     609 SVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.09e-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: 118.53  E-value: 1.09e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     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 1.12e-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: 118.57  E-value: 1.12e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5932012      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 4.22e-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: 113.90  E-value: 4.22e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   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 2.14e-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: 108.89  E-value: 2.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012   279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 277-346 2.66e-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: 108.94  E-value: 2.66e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012      277 NEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 281-346 3.31e-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: 105.43  E-value: 3.31e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     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 8.80e-25

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: 98.89  E-value: 8.80e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012      63 RLKTFETY--DTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 128
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 61-129 2.81e-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: 91.56  E-value: 2.81e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5932012    61 AKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 59-129 1.52e-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: 83.91  E-value: 1.52e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5932012       59 SEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
450-918 1.88e-19

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 95.26  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   450 QEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPDQGLANIICAQLLGAGGC 529
Cdd:COG5635  167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   530 ISEVclsssIQQL--QHQVLFLLDDY------SGLASLPQALHTLITKnyLSRTCLLIAVHTNRVRDIRLYLGTSLEIQE 601
Cdd:COG5635  245 PEDA-----LERLlrNGRLLLLLDGLdevpdeADRDEVLNQLRRFLER--YPKARVIITSRPEGYDSSELEGFEVLELAP 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   602 FPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNAS-AQDKFQdvtLFQSYMQYLSLKYK 680
Cdd:COG5635  318 LSDEQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGElPDTRAE---LYEQFVELLLERWD 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   681 ATAEPLQATVSS-------CGQLALTGLFSSCFEFNSDDL-------------AEAGVDEDEKLTTLLMskftaQRLRPV 740
Cdd:COG5635  395 EQRGLTIYRELSreelrelLSELALAMQENGRTEFAREELeeilreylgrrkdAEALLDELLLRTGLLV-----ERGEGR 469

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   741 YRFLGPLFQEFLAAVRLTELLSSDRQEdqdlglyylrQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLqlvDEKE 820
Cdd:COG5635  470 YSFAHRSFQEYLAARALVEELDEELLE----------LLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALL---ARDD 536

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   821 SLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESSSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGKTLALRVLN 900
Cdd:COG5635  537 AAALALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLL 616

                        490
                 ....*....|....*...
gi 5932012   901 LQYFRDHPESLLLLRSLK 918
Cdd:COG5635  617 ALALLLALLLLLLLLLLA 634
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 688-743 5.03e-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: 44.86  E-value: 5.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDeKLTTLLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1072-1271 1.30e-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: 48.09  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1072 LLLTLPALQSLEVSETNQLPEQLFHNLHKfLGLKElCVRLDGKPDVLSvlpgefpNLHHMEKLSIRTSTESDLSKLVKFI 1151
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1152 QNFPNLHVFHLK-CDFLSNcESLMAVLASCKKLREIEFsGRCFEAmtfvnILPNFVSLKIL-----NLKDQQFPDKETSE 1225
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD-SGIVALATNCPKLQTINL-GRHRNG-----HLITDVSLSALgknctFLQTVGFAGCDVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5932012  1226 KFAQALGSLR--NLEELLVP-----TGDGIHQVakLIVRQClqlPCLRVLTFH 1271
Cdd:cd09293  148 KGVWELASGCskSLERLSLNncrnlTDQSIPAI--LASNYF---PNLSVLEFR 195
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1118-1336 2.01e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1118 LSVLPGEFPNLHHMEKLSIRtstESDLSKLVKFIQNFPNLHVFHLKCDFLSnceSLMAVLASCKKLREIEFSGRCFEAMT 1197
Cdd:COG4886  125 LTDLPEELANLTNLKELDLS---NNQLTDLPEPLGNLTNLKSLDLSNNQLT---DLPEELGNLTNLKELDLSNNQITDLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1198 FVniLPNFVSLKILNLKDQQFpdketsEKFAQALGSLRNLEELLVpTGDGIHQVAKLivrqcLQLPCLRVLtfhdILDDD 1277
Cdd:COG4886  199 EP--LGNLTNLEELDLSGNQL------TDLPEPLANLTNLETLDL-SNNQLTDLPEL-----GNLTNLEEL----DLSNN 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 5932012  1278 SVIEIaraATSGGFQKLENLDISMNhKITEEGYRNFFQALDNLPNLQELNICRNIPGRI 1336
Cdd:COG4886  261 QLTDL---PPLANLTNLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 445-567 8.98e-05

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: 44.62  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   445 ISQPVQEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSITpDQGLANI 518
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5932012   519 ICAQLLG--AGGCISEVCLSSSIQQLQHQVLFLLDDYS-GLAslPQALHTLI 567
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
 
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 5.87e-41

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: 146.27  E-value: 5.87e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     767 EDQDLGLYYLRQIDSPLKAINSFNIFLYYvSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVR 846
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79

                           90       100
                   ....*....|....*....|....*..
gi 5932012     847 GLWLVSPESSSSFVSEHLLRLALIFAY 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 6.01e-40

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: 145.91  E-value: 6.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     464 SVMCVEGETGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSSIQ 540
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012     541 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTS--LEIQEFPFYNTV 608
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156

                          170
                   ....*....|
gi 5932012     609 SVLRKFFSHD 618
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 162-228 1.09e-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: 118.53  E-value: 1.09e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     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 1.12e-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: 118.57  E-value: 1.12e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5932012      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 4.22e-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: 113.90  E-value: 4.22e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   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 2.14e-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: 108.89  E-value: 2.14e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012   279 ELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 277-346 2.66e-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: 108.94  E-value: 2.66e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012      277 NEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
 281-346 3.31e-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: 105.43  E-value: 3.31e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     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 8.80e-25

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: 98.89  E-value: 8.80e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012      63 RLKTFETY--DTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQ 128
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
 61-129 2.81e-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: 91.56  E-value: 2.81e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5932012    61 AKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
 59-129 1.52e-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: 83.91  E-value: 1.52e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5932012       59 SEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQG 129
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
450-918 1.88e-19

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 95.26  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   450 QEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPDQGLANIICAQLLGAGGC 529
Cdd:COG5635  167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   530 ISEVclsssIQQL--QHQVLFLLDDY------SGLASLPQALHTLITKnyLSRTCLLIAVHTNRVRDIRLYLGTSLEIQE 601
Cdd:COG5635  245 PEDA-----LERLlrNGRLLLLLDGLdevpdeADRDEVLNQLRRFLER--YPKARVIITSRPEGYDSSELEGFEVLELAP 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   602 FPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNAS-AQDKFQdvtLFQSYMQYLSLKYK 680
Cdd:COG5635  318 LSDEQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGElPDTRAE---LYEQFVELLLERWD 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   681 ATAEPLQATVSS-------CGQLALTGLFSSCFEFNSDDL-------------AEAGVDEDEKLTTLLMskftaQRLRPV 740
Cdd:COG5635  395 EQRGLTIYRELSreelrelLSELALAMQENGRTEFAREELeeilreylgrrkdAEALLDELLLRTGLLV-----ERGEGR 469

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   741 YRFLGPLFQEFLAAVRLTELLSSDRQEdqdlglyylrQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLqlvDEKE 820
Cdd:COG5635  470 YSFAHRSFQEYLAARALVEELDEELLE----------LLAEHLEDPRWREVLLLLAGLLDDVKQIKELIDALL---ARDD 536

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   821 SLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESSSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGKTLALRVLN 900
Cdd:COG5635  537 AAALALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLL 616

                        490
                 ....*....|....*...
gi 5932012   901 LQYFRDHPESLLLLRSLK 918
Cdd:COG5635  617 ALALLLALLLLLLLLLLA 634
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 688-743 5.03e-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: 44.86  E-value: 5.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 5932012     688 ATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDeKLTTLLMSKFTAQRL--RPVYRF 743
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1072-1271 1.30e-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: 48.09  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1072 LLLTLPALQSLEVSETNQLPEQLFHNLHKfLGLKElCVRLDGKPDVLSvlpgefpNLHHMEKLSIRTSTESDLSKLVKFI 1151
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1152 QNFPNLHVFHLK-CDFLSNcESLMAVLASCKKLREIEFsGRCFEAmtfvnILPNFVSLKIL-----NLKDQQFPDKETSE 1225
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD-SGIVALATNCPKLQTINL-GRHRNG-----HLITDVSLSALgknctFLQTVGFAGCDVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5932012  1226 KFAQALGSLR--NLEELLVP-----TGDGIHQVakLIVRQClqlPCLRVLTFH 1271
Cdd:cd09293  148 KGVWELASGCskSLERLSLNncrnlTDQSIPAI--LASNYF---PNLSVLEFR 195
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1118-1336 2.01e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1118 LSVLPGEFPNLHHMEKLSIRtstESDLSKLVKFIQNFPNLHVFHLKCDFLSnceSLMAVLASCKKLREIEFSGRCFEAMT 1197
Cdd:COG4886  125 LTDLPEELANLTNLKELDLS---NNQLTDLPEPLGNLTNLKSLDLSNNQLT---DLPEELGNLTNLKELDLSNNQITDLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1198 FVniLPNFVSLKILNLKDQQFpdketsEKFAQALGSLRNLEELLVpTGDGIHQVAKLivrqcLQLPCLRVLtfhdILDDD 1277
Cdd:COG4886  199 EP--LGNLTNLEELDLSGNQL------TDLPEPLANLTNLETLDL-SNNQLTDLPEL-----GNLTNLEEL----DLSNN 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 5932012  1278 SVIEIaraATSGGFQKLENLDISMNhKITEEGYRNFFQALDNLPNLQELNICRNIPGRI 1336
Cdd:COG4886  261 QLTDL---PPLANLTNLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1063-1331 4.72e-05

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: 46.96  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1063 LELSRAEQELLLtLPALQSLEVSETNqLPE----QLFHNLHKFLGLKELCVRLD---GKPDVLSVLPGEFPNLHHMEKLS 1135
Cdd:cd00116   10 LKTERATELLPK-LLCLQVLRLEGNT-LGEeaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQELD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1136 IRTSTES-DLSKLVKFIQNFPNLHVFHLkcdfLSNCESLMAVLASCKKLREIE------------FSGRCFEAMTfvNIL 1202
Cdd:cd00116   88 LSDNALGpDGCGVLESLLRSSSLQELKL----NNNGLGDRGLRLLAKGLKDLPpaleklvlgrnrLEGASCEALA--KAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1203 PNFVSLKILNLKDQQFPDkETSEKFAQALGSLRNLEEL-LVPTG---DGIHQVAKLIvrqcLQLPCLRVLTFHD-ILDDD 1277
Cdd:cd00116  162 RANRDLKELNLANNGIGD-AGIRALAEGLKANCNLEVLdLNNNGltdEGASALAETL----ASLKSLEVLNLGDnNLTDA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5932012  1278 SVIEIARAATSGGfQKLENLDISMNHkITEEGYRNFFQALDNLPNLQELNICRN 1331
Cdd:cd00116  237 GAAALASALLSPN-ISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLRGN 288
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 445-567 8.98e-05

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: 44.62  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012   445 ISQPVQEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSITpDQGLANI 518
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5932012   519 ICAQLLG--AGGCISEVCLSSSIQQLQHQVLFLLDDYS-GLAslPQALHTLI 567
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1134-1365 1.59e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.69  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1134 LSIRTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMAVLASCKKLREIEFSGRcfeamtfvNILPNFVSLKILNL 1213
Cdd:COG4886   49 LTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN--------EELSNLTNLESLDL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1214 KDQQFPDketsekFAQALGSLRNLEELLVpTGDGIHQVAKLIVrqclQLPCLRVLTfhdiLDDDSVIEIARAAtsGGFQK 1293
Cdd:COG4886  121 SGNQLTD------LPEELANLTNLKELDL-SNNQLTDLPEPLG----NLTNLKSLD----LSNNQLTDLPEEL--GNLTN 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5932012  1294 LENLDISMNhKITEegyrnFFQALDNLPNLQELNICRN----IPGRIQvQATTVKAL---GQCVSRLPSLIRLHMLSWL 1365
Cdd:COG4886  184 LKELDLSNN-QITD-----LPEPLGNLTNLEELDLSGNqltdLPEPLA-NLTNLETLdlsNNQLTDLPELGNLTNLEEL 255
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1058-1331 1.10e-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: 43.24  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1058 CSMSRLELsrAEQELLLTLPALQsLEVSETNQLPE--QLFHNLHKFLGLKELCVRLDGKPDVLSvlpGEFPN------LH 1129
Cdd:COG5238   98 EEVSPVAL--AETATAVATPPPD-LRRIMAKTLEDslILYLALPRRINLIQVLKDPLGGNAVHL---LGLAArlgllaAI 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1130 HMEKLSIRTSTES-DLS----------KLVKFIQNFPNLHVFHLKCDFL--SNCESLMAVLASCKKLREIEFSGRCF--- 1193
Cdd:COG5238  172 SMAKALQNNSVETvYLGcnqigdegieELAEALTQNTTVTTLWLKRNPIgdEGAEILAEALKGNKSLTTLDLSNNQIgde 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5932012  1194 EAMTFVNILPNFVSLKILNLKDQQFpDKETSEKFAQALGSLRNLEELLV---PTGD-GIHQVAK-LIVRQCLQLPCLRvl 1268
Cdd:COG5238  252 GVIALAEALKNNTTVETLYLSGNQI-GAEGAIALAKALQGNTTLTSLDLsvnRIGDeGAIALAEgLQGNKTLHTLNLA-- 328

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5932012  1269 tfHDILDDDSVIEIARAATSGgfQKLENLDISMNhKITEEGYRNFFQALDNLPNLQELNICRN 1331
Cdd:COG5238  329 --YNGIGAQGAIALAKALQEN--TTLHSLDLSDN-QIGDEGAIALAKYLEGNTTLRELNLGKN 386
 
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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