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Conserved domains on  [gi|1039753651|ref|XP_017172980|]
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NLR family CARD domain-containing protein 4 isoform X1 [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 ...
465-579 6.96e-35

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: 128.55  E-value: 6.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  465 EEVSKGNSYLNKMVSISDITSLYGNLLLYTCGSSTEATRAVMRHLAMVYQH-GSLQGLSvtkrplwrqESIQSLRNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753651  544 DVLKAiNVNSFVECGINLFSESMSKSDLSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-310 1.16e-28

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: 112.78  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  163 SPCLIEGESGKGKSTLLQRIAMLWASGGCRalKGFRLVFFIHLRSARG-----GLFETLYDQLLNIPDFIskPTFKALLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP--QGFDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPV--SEVWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  238 KLHKEVLFLLDGYNEFHPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRH--VGALTAEVGDMTEDSAK 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRglEEPRYLEVRGFSESDRK 156

                   ....
gi 1039753651  307 DLIE 310
Cdd:pfam05729  157 QYVR 160
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 2.97e-27

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 119.52  E-value: 2.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  148 RVEQLTLGSLLEALKSPCLIEGESGKGKSTLLQRIAMLWASGGCRALKgfRLVFFIHLRSARGG--LFETLYDQLLNIPD 225
Cdd:COG5635    166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAED--PIPILIELRDLAEEasLEDLLAEALEKRGG 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  226 fISKPTFKALLlkLHKEVLFLLDGYNEFHPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRHVGALTAEVGDM 300
Cdd:COG5635    244 -EPEDALERLL--RNGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  301 TEDSAKDLIEA--VLVPDQVERLWAQIQESRCLRNLMKTPLFVVITCAIQMGRQEFqAHTQTMLFQTFYDLLIQK-NSHR 377
Cdd:COG5635    319 SDEQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLERwDEQR 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  378 YRGGASG-DFARSLDYCGDLALEGVFAHKFDFEPE--------------HGSSMNEDVLVTIGLLCkytaQRLKPTYKFF 442
Cdd:COG5635    398 GLTIYRElSREELRELLSELALAMQENGRTEFAREeleeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSFA 473
                          330       340
                   ....*....|....*....|....*..
gi 1039753651  443 HKSFQEYTAGRRLSSLLTSKEPEEVSK 469
Cdd:COG5635    474 HRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 7.69e-16

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


:

Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 73.36  E-value: 7.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651    1 MNFIRNNRRALIQRmgLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFV 80
Cdd:pfam00619    1 RKLLKKNRVALVER--LGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 1039753651   81 YQDLTGQ 87
Cdd:pfam00619   79 ASDLEGL 85
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
660-888 1.47e-09

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: 61.34  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  660 KTLEVTLRDINKLNKQDIKYLGKIFSSATNLR-LHIKRCA---AMAGRLSSVLRTCKNMHTLMVEASPLttDDEQYITSV 735
Cdd:COG5238    180 NSVETVYLGCNQIGDEGIEELAEALTQNTTVTtLWLKRNPigdEGAEILAEALKGNKSLTTLDLSNNQI--GDEGVIALA 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  736 TGLQ-NLSIHRLH------TQQLPGGLIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHlSDIG-EG 807
Cdd:COG5238    258 EALKnNTTVETLYlsgnqiGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-NGIGaQG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  808 MDYIVKSLSE----ESCDLQEMKlvaccLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELIgrlgVLGELTT 883
Cdd:COG5238    337 AIALAKALQEnttlHSLDLSDNQ-----IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL----QTNRLHT 407

                   ....*
gi 1039753651  884 LMLPW 888
Cdd:COG5238    408 LILDG 412
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
465-579 6.96e-35

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: 128.55  E-value: 6.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  465 EEVSKGNSYLNKMVSISDITSLYGNLLLYTCGSSTEATRAVMRHLAMVYQH-GSLQGLSvtkrplwrqESIQSLRNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753651  544 DVLKAiNVNSFVECGINLFSESMSKSDLSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-310 1.16e-28

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: 112.78  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  163 SPCLIEGESGKGKSTLLQRIAMLWASGGCRalKGFRLVFFIHLRSARG-----GLFETLYDQLLNIPDFIskPTFKALLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP--QGFDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPV--SEVWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  238 KLHKEVLFLLDGYNEFHPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRH--VGALTAEVGDMTEDSAK 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRglEEPRYLEVRGFSESDRK 156

                   ....
gi 1039753651  307 DLIE 310
Cdd:pfam05729  157 QYVR 160
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 2.97e-27

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 119.52  E-value: 2.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  148 RVEQLTLGSLLEALKSPCLIEGESGKGKSTLLQRIAMLWASGGCRALKgfRLVFFIHLRSARGG--LFETLYDQLLNIPD 225
Cdd:COG5635    166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAED--PIPILIELRDLAEEasLEDLLAEALEKRGG 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  226 fISKPTFKALLlkLHKEVLFLLDGYNEFHPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRHVGALTAEVGDM 300
Cdd:COG5635    244 -EPEDALERLL--RNGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  301 TEDSAKDLIEA--VLVPDQVERLWAQIQESRCLRNLMKTPLFVVITCAIQMGRQEFqAHTQTMLFQTFYDLLIQK-NSHR 377
Cdd:COG5635    319 SDEQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLERwDEQR 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  378 YRGGASG-DFARSLDYCGDLALEGVFAHKFDFEPE--------------HGSSMNEDVLVTIGLLCkytaQRLKPTYKFF 442
Cdd:COG5635    398 GLTIYRElSREELRELLSELALAMQENGRTEFAREeleeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSFA 473
                          330       340
                   ....*....|....*....|....*..
gi 1039753651  443 HKSFQEYTAGRRLSSLLTSKEPEEVSK 469
Cdd:COG5635    474 HRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 7.69e-16

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 73.36  E-value: 7.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651    1 MNFIRNNRRALIQRmgLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFV 80
Cdd:pfam00619    1 RKLLKKNRVALVER--LGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 1039753651   81 YQDLTGQ 87
Cdd:pfam00619   79 ASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
4-78 1.04e-09

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 55.99  E-value: 1.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753651    4 IRNNRRALIQRMgltVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDY 78
Cdd:cd01671      1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQ 72
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
660-888 1.47e-09

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: 61.34  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  660 KTLEVTLRDINKLNKQDIKYLGKIFSSATNLR-LHIKRCA---AMAGRLSSVLRTCKNMHTLMVEASPLttDDEQYITSV 735
Cdd:COG5238    180 NSVETVYLGCNQIGDEGIEELAEALTQNTTVTtLWLKRNPigdEGAEILAEALKGNKSLTTLDLSNNQI--GDEGVIALA 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  736 TGLQ-NLSIHRLH------TQQLPGGLIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHlSDIG-EG 807
Cdd:COG5238    258 EALKnNTTVETLYlsgnqiGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-NGIGaQG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  808 MDYIVKSLSE----ESCDLQEMKlvaccLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELIgrlgVLGELTT 883
Cdd:COG5238    337 AIALAKALQEnttlHSLDLSDNQ-----IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL----QTNRLHT 407

                   ....*
gi 1039753651  884 LMLPW 888
Cdd:COG5238    408 LILDG 412
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
755-871 2.41e-08

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: 56.98  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  755 LIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHLSDIGEGMDYIVKSLSEESCDLQEMKLVACCLTA 834
Cdd:cd00116    185 LAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITD 264
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039753651  835 NSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQEL 871
Cdd:cd00116    265 DGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
465-579 6.96e-35

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: 128.55  E-value: 6.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  465 EEVSKGNSYLNKMVSISDITSLYGNLLLYTCGSSTEATRAVMRHLAMVYQH-GSLQGLSvtkrplwrqESIQSLRNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039753651  544 DVLKAiNVNSFVECGINLFSESMSKSDLSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-310 1.16e-28

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: 112.78  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  163 SPCLIEGESGKGKSTLLQRIAMLWASGGCRalKGFRLVFFIHLRSARG-----GLFETLYDQLLNIPDFIskPTFKALLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP--QGFDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPV--SEVWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  238 KLHKEVLFLLDGYNEFHPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRH--VGALTAEVGDMTEDSAK 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRglEEPRYLEVRGFSESDRK 156

                   ....
gi 1039753651  307 DLIE 310
Cdd:pfam05729  157 QYVR 160
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 2.97e-27

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 119.52  E-value: 2.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  148 RVEQLTLGSLLEALKSPCLIEGESGKGKSTLLQRIAMLWASGGCRALKgfRLVFFIHLRSARGG--LFETLYDQLLNIPD 225
Cdd:COG5635    166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAED--PIPILIELRDLAEEasLEDLLAEALEKRGG 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  226 fISKPTFKALLlkLHKEVLFLLDGYNEFHPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRHVGALTAEVGDM 300
Cdd:COG5635    244 -EPEDALERLL--RNGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  301 TEDSAKDLIEA--VLVPDQVERLWAQIQESRCLRNLMKTPLFVVITCAIQMGRQEFqAHTQTMLFQTFYDLLIQK-NSHR 377
Cdd:COG5635    319 SDEQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLERwDEQR 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  378 YRGGASG-DFARSLDYCGDLALEGVFAHKFDFEPE--------------HGSSMNEDVLVTIGLLCkytaQRLKPTYKFF 442
Cdd:COG5635    398 GLTIYRElSREELRELLSELALAMQENGRTEFAREeleeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSFA 473
                          330       340
                   ....*....|....*....|....*..
gi 1039753651  443 HKSFQEYTAGRRLSSLLTSKEPEEVSK 469
Cdd:COG5635    474 HRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 7.69e-16

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 73.36  E-value: 7.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651    1 MNFIRNNRRALIQRmgLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFV 80
Cdd:pfam00619    1 RKLLKKNRVALVER--LGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 1039753651   81 YQDLTGQ 87
Cdd:pfam00619   79 ASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
4-78 1.04e-09

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 55.99  E-value: 1.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753651    4 IRNNRRALIQRMgltVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDY 78
Cdd:cd01671      1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQ 72
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
660-888 1.47e-09

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: 61.34  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  660 KTLEVTLRDINKLNKQDIKYLGKIFSSATNLR-LHIKRCA---AMAGRLSSVLRTCKNMHTLMVEASPLttDDEQYITSV 735
Cdd:COG5238    180 NSVETVYLGCNQIGDEGIEELAEALTQNTTVTtLWLKRNPigdEGAEILAEALKGNKSLTTLDLSNNQI--GDEGVIALA 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  736 TGLQ-NLSIHRLH------TQQLPGGLIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHlSDIG-EG 807
Cdd:COG5238    258 EALKnNTTVETLYlsgnqiGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-NGIGaQG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  808 MDYIVKSLSE----ESCDLQEMKlvaccLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELIgrlgVLGELTT 883
Cdd:COG5238    337 AIALAKALQEnttlHSLDLSDNQ-----IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL----QTNRLHT 407

                   ....*
gi 1039753651  884 LMLPW 888
Cdd:COG5238    408 LILDG 412
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
3-87 5.77e-09

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 54.37  E-value: 5.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651    3 FIRNNRRALIQRmgLTVTKQICDDLFALNVLNNQEANVIYCEPLEQEAARKIIHMTMQKGSAACNLFLKSLENWDYFVYQ 82
Cdd:cd08329     10 LIRKNRMALFQH--LTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87

                   ....*
gi 1039753651   83 DLTGQ 87
Cdd:cd08329     88 DLFVQ 92
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
755-871 2.41e-08

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: 56.98  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  755 LIDSLGNLKNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHLSDIGEGMDYIVKSLSEESCDLQEMKLVACCLTA 834
Cdd:cd00116    185 LAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITD 264
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039753651  835 NSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQEL 871
Cdd:cd00116    265 DGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
738-1009 2.17e-07

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: 53.90  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  738 LQNLSIHRLHTQQLPGGLIDSLGNLKNLERLILDDIRMNE--EDAKNLAEGLRSLKKMRLLHLTHLSDIGEGMDYIVKSL 815
Cdd:cd00116     53 LKELCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNAlgPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  816 SEESCDLQEMKLVACCLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELigrLGVLGELTTLMLPWCWDVHTS 895
Cdd:cd00116    133 KDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEG---LKANCNLEVLDLNNNGLTDEG 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  896 LPKLLKQLEGTPGLAKLGLKNWRLRDEEIKSLGEFLEMnPLRDLQQLDLAGHCVSSDGWLYFMNVFENLKQLVFFDFSTE 975
Cdd:cd00116    210 ASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLS-PNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1039753651  976 EFLPDAAlvrklsQVLSKLTLLQEVKL-TGWEFDD 1009
Cdd:cd00116    289 KFGEEGA------QLLAESLLEPGNELeSLWVKDD 317
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
747-973 2.20e-06

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: 51.33  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  747 HTQQLPGGLIDSLGNL-KNLERLILDDIRMNEEDAKNLAEGLRSLKKMRLLHLTHLSdIG-EGMDYIVKSLSEEScDLQE 824
Cdd:COG5238    163 ARLGLLAAISMAKALQnNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNP-IGdEGAEILAEALKGNK-SLTT 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753651  825 MKLVACCLTANSVKVLAQNLHNLIKLSILDISENYLEKDGNEALQELigrLGVLGELTTLMLpwcWDVHTSLP---KLLK 901
Cdd:COG5238    241 LDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKA---LQGNTTLTSLDL---SVNRIGDEgaiALAE 314
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753651  902 QLEGTPGLAKLGLKNWRLRDEEIKSLGEFLEMNplRDLQQLDLAGHCVSSDGWLYFMNVFENLKQLVFFDFS 973
Cdd:COG5238    315 GLQGNKTLHTLNLAYNGIGAQGAIALAKALQEN--TTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLG 384
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
5-77 6.17e-03

Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260036  Cd Length: 83  Bit Score: 36.80  E-value: 6.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753651    5 RNNRRALIQRMGLTVTKQICDDLFALNVLNNQEANVIYCE-PLEQEAARKIIHMTMQKGSAACNLFLKSLENWD 77
Cdd:cd08325      3 KEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEEnNTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRD 76
 
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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