|
Name |
Accession |
Description |
Interval |
E-value |
| NLRC4_HD |
pfam17889 |
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ... |
604-710 |
1.63e-52 |
|
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: 179.02 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 604 EHQDLGLYHLKQINSPMMTVSAYNNFLNYvSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLR 683
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
|
90 100
....*....|....*....|....*..
gi 119393876 684 GLWQICPQAYFSMVSEHLLVLALKTAY 710
Cdd:pfam17889 80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
302-455 |
1.60e-42 |
|
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: 152.84 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 302 SVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLnrFQLVFYLSLSSTRPDE---GLASIICDQLLEKEGSVTEmcVRNIIQ 378
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 379 QLKNQVLFLLDDYKEICSIPQ----------VIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLET--ILEIKAFPFYNTV 446
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGqldgpcpvltLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEprYLEVRGFSESDRK 156
|
....*....
gi 119393876 447 CILRKLFSH 455
Cdd:pfam05729 157 QYVRKYFSD 165
|
|
| BIR |
smart00238 |
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ... |
116-185 |
9.85e-32 |
|
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: 9.85e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 116 EELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQN 185
Cdd:smart00238 2 EEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
288-604 |
1.28e-18 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
:
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 92.18 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 288 QEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRfqLVFYLSLSSTRPDEGLASIICDQLLEKEGS 367
Cdd:COG5635 167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 368 VTEmcvrNIIQQLKN-QVLFLLDDYKEI---CSIPQVIGKLIQ-KNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPF 442
Cdd:COG5635 245 PED----ALERLLRNgRLLLLLDGLDEVpdeADRDEVLNQLRRfLERYPKARVIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 443 YNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSfDDVAVFKSYMERLSLRNKATAEI 522
Cdd:COG5635 321 EQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPD-TRAELYEQFVELLLERWDEQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 523 LKATVSS-------CGELALKGFFSCCFEFNDDDLAE-------AGVDEDEDLTMCLMSKF----TAQRLrpfYRFLSPA 584
Cdd:COG5635 400 TIYRELSreelrelLSELALAMQENGRTEFAREELEEilreylgRRKDAEALLDELLLRTGllveRGEGR---YSFAHRS 476
|
330 340
....*....|....*....|
gi 119393876 585 FQEFLAGMRLIELLDSDRQE 604
Cdd:COG5635 477 FQEYLAARALVEELDEELLE 496
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
988-1218 |
1.29e-05 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
The actual alignment was detected with superfamily member COG5238:
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 49.02 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 988 LIQNsPNLHVFHLKCNFFSDFGS--LMTMLVSCKKLTEIKFSDSFFQAVPFVA---SLPNFISLKILNLEGQQFpDEETS 1062
Cdd:COG5238 204 LTQN-TTVTTLWLKRNPIGDEGAeiLAEALKGNKSLTTLDLSNNQIGDEGVIAlaeALKNNTTVETLYLSGNQI-GAEGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1063 EKFAYILGSLSNLEELIL---PTGDgiyRVAKLIIQQCQQLHCLRVLSFFKT-LNDDSVVEIAKvAISGGfQKLENLKLS 1138
Cdd:COG5238 282 IALAKALQGNTTLTSLDLsvnRIGD---EGAIALAEGLQGNKTLHTLNLAYNgIGAQGAIALAK-ALQEN-TTLHSLDLS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1139 INhKITEEGYRNFFQALDNMPNLQELDISRH------FTECIKAQATTvkslsqcvlrlpRLIRLNMLSWLLDADDIALL 1212
Cdd:COG5238 357 DN-QIGDEGAIALAKYLEGNTTLRELNLGKNnigkqgAEALIDALQTN------------RLHTLILDGNLIGAEAQQRL 423
|
....*.
gi 119393876 1213 NVMKER 1218
Cdd:COG5238 424 EQLLER 429
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NLRC4_HD |
pfam17889 |
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ... |
604-710 |
1.63e-52 |
|
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: 179.02 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 604 EHQDLGLYHLKQINSPMMTVSAYNNFLNYvSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLR 683
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
|
90 100
....*....|....*....|....*..
gi 119393876 684 GLWQICPQAYFSMVSEHLLVLALKTAY 710
Cdd:pfam17889 80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
302-455 |
1.60e-42 |
|
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: 152.84 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 302 SVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLnrFQLVFYLSLSSTRPDE---GLASIICDQLLEKEGSVTEmcVRNIIQ 378
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 379 QLKNQVLFLLDDYKEICSIPQ----------VIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLET--ILEIKAFPFYNTV 446
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGqldgpcpvltLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEprYLEVRGFSESDRK 156
|
....*....
gi 119393876 447 CILRKLFSH 455
Cdd:pfam05729 157 QYVRKYFSD 165
|
|
| BIR |
smart00238 |
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ... |
116-185 |
9.85e-32 |
|
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: 9.85e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 116 EELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQN 185
Cdd:smart00238 2 EEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
|
|
| BIR |
cd00022 |
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ... |
117-185 |
1.75e-31 |
|
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: 117.75 E-value: 1.75e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119393876 117 ELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQN 185
Cdd:cd00022 1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
|
|
| BIR |
pfam00653 |
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ... |
119-184 |
1.37e-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: 106.59 E-value: 1.37e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119393876 119 RLDSFKDWPRESAVGVA--ALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQ 184
Cdd:pfam00653 1 RLATFENWPHSNKSPPTpeELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
288-604 |
1.28e-18 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 92.18 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 288 QEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRfqLVFYLSLSSTRPDEGLASIICDQLLEKEGS 367
Cdd:COG5635 167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 368 VTEmcvrNIIQQLKN-QVLFLLDDYKEI---CSIPQVIGKLIQ-KNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPF 442
Cdd:COG5635 245 PED----ALERLLRNgRLLLLLDGLDEVpdeADRDEVLNQLRRfLERYPKARVIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 443 YNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSfDDVAVFKSYMERLSLRNKATAEI 522
Cdd:COG5635 321 EQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPD-TRAELYEQFVELLLERWDEQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 523 LKATVSS-------CGELALKGFFSCCFEFNDDDLAE-------AGVDEDEDLTMCLMSKF----TAQRLrpfYRFLSPA 584
Cdd:COG5635 400 TIYRELSreelrelLSELALAMQENGRTEFAREELEEilreylgRRKDAEALLDELLLRTGllveRGEGR---YSFAHRS 476
|
330 340
....*....|....*....|
gi 119393876 585 FQEFLAGMRLIELLDSDRQE 604
Cdd:COG5635 477 FQEYLAARALVEELDEELLE 496
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
988-1218 |
1.29e-05 |
|
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: 49.02 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 988 LIQNsPNLHVFHLKCNFFSDFGS--LMTMLVSCKKLTEIKFSDSFFQAVPFVA---SLPNFISLKILNLEGQQFpDEETS 1062
Cdd:COG5238 204 LTQN-TTVTTLWLKRNPIGDEGAeiLAEALKGNKSLTTLDLSNNQIGDEGVIAlaeALKNNTTVETLYLSGNQI-GAEGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1063 EKFAYILGSLSNLEELIL---PTGDgiyRVAKLIIQQCQQLHCLRVLSFFKT-LNDDSVVEIAKvAISGGfQKLENLKLS 1138
Cdd:COG5238 282 IALAKALQGNTTLTSLDLsvnRIGD---EGAIALAEGLQGNKTLHTLNLAYNgIGAQGAIALAK-ALQEN-TTLHSLDLS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1139 INhKITEEGYRNFFQALDNMPNLQELDISRH------FTECIKAQATTvkslsqcvlrlpRLIRLNMLSWLLDADDIALL 1212
Cdd:COG5238 357 DN-QIGDEGAIALAKYLEGNTTLRELNLGKNnigkqgAEALIDALQTN------------RLHTLILDGNLIGAEAQQRL 423
|
....*.
gi 119393876 1213 NVMKER 1218
Cdd:COG5238 424 EQLLER 429
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
301-438 |
1.70e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 301 NSVMCVEGEAGSGKTVLLKKIAFLwasgccpLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQL 380
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119393876 381 KNQ---VLFL------LDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVrTNRARD-----IRRYLETILEIK 438
Cdd:smart00382 75 RKLkpdVLILdeitslLDAEQEALLLLLEELRLLLLLKSEKNLTVILT-TNDEKDlgpalLRRRFDRRIVLL 145
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1009-1212 |
5.75e-04 |
|
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: 43.50 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1009 GSLMTMLVSCKKLTEIKFSDSFFQA--VPFVASLPNFISLKILNLEgqQFPDEETSEKFayILGSLSNLEElilptgdgi 1086
Cdd:cd00116 71 QSLLQGLTKGCGLQELDLSDNALGPdgCGVLESLLRSSSLQELKLN--NNGLGDRGLRL--LAKGLKDLPP--------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1087 yRVAKLIIQQCqqlhclrvlsffkTLNDDSVVEIAKVAISGGfqKLENLKLSINHkITEEGYRNFFQALDNMPNLQELDI 1166
Cdd:cd00116 138 -ALEKLVLGRN-------------RLEGASCEALAKALRANR--DLKELNLANNG-IGDAGIRALAEGLKANCNLEVLDL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 119393876 1167 SRHFTECIKAQAttvksLSQCVLRLPRLIRLNMLSWLLDADDIALL 1212
Cdd:cd00116 201 NNNGLTDEGASA-----LAETLASLKSLEVLNLGDNNLTDAGAAAL 241
|
|
| NOD2_WH |
pfam17779 |
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
525-580 |
8.12e-04 |
|
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: 38.70 E-value: 8.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119393876 525 ATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDeDLTMCLMSKFTAQRL--RPFYRF 580
Cdd:pfam17779 1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NLRC4_HD |
pfam17889 |
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ... |
604-710 |
1.63e-52 |
|
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: 179.02 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 604 EHQDLGLYHLKQINSPMMTVSAYNNFLNYvSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLR 683
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
|
90 100
....*....|....*....|....*..
gi 119393876 684 GLWQICPQAYFSMVSEHLLVLALKTAY 710
Cdd:pfam17889 80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
302-455 |
1.60e-42 |
|
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: 152.84 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 302 SVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLnrFQLVFYLSLSSTRPDE---GLASIICDQLLEKEGSVTEmcVRNIIQ 378
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 379 QLKNQVLFLLDDYKEICSIPQ----------VIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLET--ILEIKAFPFYNTV 446
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGqldgpcpvltLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEprYLEVRGFSESDRK 156
|
....*....
gi 119393876 447 CILRKLFSH 455
Cdd:pfam05729 157 QYVRKYFSD 165
|
|
| BIR |
smart00238 |
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ... |
116-185 |
9.85e-32 |
|
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: 9.85e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 116 EELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQN 185
Cdd:smart00238 2 EEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
|
|
| BIR |
cd00022 |
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ... |
117-185 |
1.75e-31 |
|
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: 117.75 E-value: 1.75e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119393876 117 ELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQN 185
Cdd:cd00022 1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
|
|
| BIR |
pfam00653 |
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ... |
119-184 |
1.37e-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: 106.59 E-value: 1.37e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119393876 119 RLDSFKDWPRESAVGVA--ALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQ 184
Cdd:pfam00653 1 RLATFENWPHSNKSPPTpeELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
288-604 |
1.28e-18 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 92.18 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 288 QEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRfqLVFYLSLSSTRPDEGLASIICDQLLEKEGS 367
Cdd:COG5635 167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 368 VTEmcvrNIIQQLKN-QVLFLLDDYKEI---CSIPQVIGKLIQ-KNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPF 442
Cdd:COG5635 245 PED----ALERLLRNgRLLLLLDGLDEVpdeADRDEVLNQLRRfLERYPKARVIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 443 YNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSfDDVAVFKSYMERLSLRNKATAEI 522
Cdd:COG5635 321 EQIEEFLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPD-TRAELYEQFVELLLERWDEQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 523 LKATVSS-------CGELALKGFFSCCFEFNDDDLAE-------AGVDEDEDLTMCLMSKF----TAQRLrpfYRFLSPA 584
Cdd:COG5635 400 TIYRELSreelrelLSELALAMQENGRTEFAREELEEilreylgRRKDAEALLDELLLRTGllveRGEGR---YSFAHRS 476
|
330 340
....*....|....*....|
gi 119393876 585 FQEFLAGMRLIELLDSDRQE 604
Cdd:COG5635 477 FQEYLAARALVEELDEELLE 496
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
988-1218 |
1.29e-05 |
|
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: 49.02 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 988 LIQNsPNLHVFHLKCNFFSDFGS--LMTMLVSCKKLTEIKFSDSFFQAVPFVA---SLPNFISLKILNLEGQQFpDEETS 1062
Cdd:COG5238 204 LTQN-TTVTTLWLKRNPIGDEGAeiLAEALKGNKSLTTLDLSNNQIGDEGVIAlaeALKNNTTVETLYLSGNQI-GAEGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1063 EKFAYILGSLSNLEELIL---PTGDgiyRVAKLIIQQCQQLHCLRVLSFFKT-LNDDSVVEIAKvAISGGfQKLENLKLS 1138
Cdd:COG5238 282 IALAKALQGNTTLTSLDLsvnRIGD---EGAIALAEGLQGNKTLHTLNLAYNgIGAQGAIALAK-ALQEN-TTLHSLDLS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1139 INhKITEEGYRNFFQALDNMPNLQELDISRH------FTECIKAQATTvkslsqcvlrlpRLIRLNMLSWLLDADDIALL 1212
Cdd:COG5238 357 DN-QIGDEGAIALAKYLEGNTTLRELNLGKNnigkqgAEALIDALQTN------------RLHTLILDGNLIGAEAQQRL 423
|
....*.
gi 119393876 1213 NVMKER 1218
Cdd:COG5238 424 EQLLER 429
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
301-438 |
1.70e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 301 NSVMCVEGEAGSGKTVLLKKIAFLwasgccpLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQL 380
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119393876 381 KNQ---VLFL------LDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVrTNRARD-----IRRYLETILEIK 438
Cdd:smart00382 75 RKLkpdVLILdeitslLDAEQEALLLLLEELRLLLLLKSEKNLTVILT-TNDEKDlgpalLRRRFDRRIVLL 145
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1045-1167 |
3.49e-04 |
|
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: 44.40 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1045 SLKILNLEGQQFpDEETSEKFAYILGSLSNLEELIL---PTGDgiyRVAKLIIQQCQQLHCLRVLSFFKT-LNDDSVVEI 1120
Cdd:COG5238 181 SVETVYLGCNQI-GDEGIEELAEALTQNTTVTTLWLkrnPIGD---EGAEILAEALKGNKSLTTLDLSNNqIGDEGVIAL 256
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119393876 1121 AKVAISGgfQKLENLKLSINHkITEEGYRNFFQALDNMPNLQELDIS 1167
Cdd:COG5238 257 AEALKNN--TTVETLYLSGNQ-IGAEGAIALAKALQGNTTLTSLDLS 300
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1009-1212 |
5.75e-04 |
|
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: 43.50 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1009 GSLMTMLVSCKKLTEIKFSDSFFQA--VPFVASLPNFISLKILNLEgqQFPDEETSEKFayILGSLSNLEElilptgdgi 1086
Cdd:cd00116 71 QSLLQGLTKGCGLQELDLSDNALGPdgCGVLESLLRSSSLQELKLN--NNGLGDRGLRL--LAKGLKDLPP--------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1087 yRVAKLIIQQCqqlhclrvlsffkTLNDDSVVEIAKVAISGGfqKLENLKLSINHkITEEGYRNFFQALDNMPNLQELDI 1166
Cdd:cd00116 138 -ALEKLVLGRN-------------RLEGASCEALAKALRANR--DLKELNLANNG-IGDAGIRALAEGLKANCNLEVLDL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 119393876 1167 SRHFTECIKAQAttvksLSQCVLRLPRLIRLNMLSWLLDADDIALL 1212
Cdd:cd00116 201 NNNGLTDEGASA-----LAETLASLKSLEVLNLGDNNLTDAGAAAL 241
|
|
| NOD2_WH |
pfam17779 |
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
525-580 |
8.12e-04 |
|
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: 38.70 E-value: 8.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119393876 525 ATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDeDLTMCLMSKFTAQRL--RPFYRF 580
Cdd:pfam17779 1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDES-DLSSGLLTEILQKDLgcEKVYSF 57
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
903-1199 |
8.47e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 43.38 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 903 LSAAEQELLLTLPSLESLEVSGTIQSQDQIFPNLDKFLCLKELSVDLEGNINVFSVIPEEFPNFHHMEKLLIQISAEYDP 982
Cdd:COG4886 6 LSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 983 SKLVKLIQNSPNLHVFHLKCNffsdfgslmTMLVSCKKLTEIKFSDSFFQAVPfvASLPNFISLKILNLEGQQFPDEETS 1062
Cdd:COG4886 86 LLGLTDLGDLTNLTELDLSGN---------EELSNLTNLESLDLSGNQLTDLP--EELANLTNLKELDLSNNQLTDLPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1063 ekfayiLGSLSNLEELILpTGDGIYRVAKLIiqqcQQLHCLRVLSffktLNDDSVVEIAKvAIsGGFQKLENLKLSINhK 1142
Cdd:COG4886 155 ------LGNLTNLKSLDL-SNNQLTDLPEEL----GNLTNLKELD----LSNNQITDLPE-PL-GNLTNLEELDLSGN-Q 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119393876 1143 ITEegyrnFFQALDNMPNLQELDISRhftecikAQATTVKSLSQcvlrLPRLIRLNM 1199
Cdd:COG4886 217 LTD-----LPEPLANLTNLETLDLSN-------NQLTDLPELGN----LTNLEELDL 257
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
911-1180 |
3.09e-03 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 41.46 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 911 LLTLPSLESLEVSGT-IQSQDQIFPNLDKflcLKELSVdlegNINVFSVIPEEFPNFHHMEKLLI---QISAeydpskLV 986
Cdd:COG4886 155 LGNLTNLKSLDLSNNqLTDLPEELGNLTN---LKELDL----SNNQITDLPEPLGNLTNLEELDLsgnQLTD------LP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 987 KLIQNSPNLHVFHLKCNFFSDFGSLMTMlvscKKLTEIKFSDSFFQAVPFVASLPNfisLKILNLEGQQFPDEETSEKFA 1066
Cdd:COG4886 222 EPLANLTNLETLDLSNNQLTDLPELGNL----TNLEELDLSNNQLTDLPPLANLTN---LKTLDLSNNQLTDLKLKELEL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393876 1067 YILGSLSNLEELILPTGDGIYRVAKLIIQQCQQLHCLRVLSFFKTLNDDSVVEIAKVAISGGFQKLENLKLSINHKITEE 1146
Cdd:COG4886 295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGL 374
|
250 260 270
....*....|....*....|....*....|....
gi 119393876 1147 GYRNFFQALDNMPNLQELDISRHFTECIKAQATT 1180
Cdd:COG4886 375 LEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408
|
|
| |
