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Conserved domains on  [gi|767944762|ref|XP_011513386|]
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nucleotide-binding oligomerization domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.81e-48

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: 167.87  E-value: 5.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 767944762  354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
 21-105 4.74e-45

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 260035  Cd Length: 85  Bit Score: 156.48  E-value: 4.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....*
gi 767944762 101 RPWLL 105
Cdd:cd08324   81 RPWLD 85
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.56e-38

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: 148.40  E-value: 3.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767944762 889 ADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 922
Cdd:COG5238  397 IDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 3.70e-21

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 99.49  E-value: 3.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635  250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635  384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767944762 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635  457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
NLRC4_HD2 super family cl39284
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 2.01e-11

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


The actual alignment was detected with superfamily member pfam17776:

Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 61.92  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767944762  597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.81e-48

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: 167.87  E-value: 5.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 767944762  354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
 21-105 4.74e-45

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 260035  Cd Length: 85  Bit Score: 156.48  E-value: 4.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....*
gi 767944762 101 RPWLL 105
Cdd:cd08324   81 RPWLD 85
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.56e-38

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: 148.40  E-value: 3.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767944762 889 ADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 922
Cdd:COG5238  397 IDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 3.70e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 99.49  E-value: 3.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635  250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635  384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767944762 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635  457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 676-914 8.40e-20

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: 91.26  E-value: 8.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGLASNGISTEG 828
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 829 GKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQS-NTGITEICLNGNL 907
Cdd:cd00116  182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCND 261


                 ....*..
gi 767944762 908 IKPEEAK 914
Cdd:cd00116  262 ITDDGAK 268
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-92 3.08e-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: 74.52  E-value: 3.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767944762   21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE 73
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 2.01e-11

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 61.92  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767944762  597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 458-515 4.06e-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: 4.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767944762  458 DTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELgPGGDQQSYEF 515
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.81e-48

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: 167.87  E-value: 5.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 767944762  354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
 21-105 4.74e-45

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 260035  Cd Length: 85  Bit Score: 156.48  E-value: 4.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....*
gi 767944762 101 RPWLL 105
Cdd:cd08324   81 RPWLD 85
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.56e-38

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: 148.40  E-value: 3.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767944762 889 ADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 922
Cdd:COG5238  397 IDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-914 6.85e-34

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: 135.69  E-value: 6.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 730 LTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVK 809
Cdd:COG5238  210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 810 NSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLA 889
Cdd:COG5238  290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                        170       180
                 ....*....|....*....|....*
gi 767944762 890 DALQSNTGITEICLNGNLIKPEEAK 914
Cdd:COG5238  370 KYLEGNTTLRELNLGKNNIGKQGAE 394
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-915 4.14e-33

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: 133.38  E-value: 4.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238  181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238  261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIAL 340

                        170       180
                 ....*....|....*....|....*..
gi 767944762 889 ADALQSNTGITEICLNGNLIKPEEAKV 915
Cdd:COG5238  341 AKALQENTTLHSLDLSDNQIGDEGAIA 367
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 3.70e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 99.49  E-value: 3.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635  250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635  384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767944762 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635  457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 676-914 8.40e-20

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: 91.26  E-value: 8.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGLASNGISTEG 828
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 829 GKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQS-NTGITEICLNGNL 907
Cdd:cd00116  182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCND 261


                 ....*..
gi 767944762 908 IKPEEAK 914
Cdd:cd00116  262 ITDDGAK 268
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 723-892 7.42e-19

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: 88.57  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 723 LQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGK 802
Cdd:cd00116  132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 803 YLALAVKNSKSISEVGLASNGISTEGGKSLARAL-QQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQIT 881
Cdd:cd00116  212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291

                        170
                 ....*....|.
gi 767944762 882 AKGTAQLADAL 892
Cdd:cd00116  292 EEGAQLLAESL 302
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 719-908 1.35e-18

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: 87.80  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 719 GVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKI------------------------------VTYLGLYNNQI 768
Cdd:cd00116   14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSlkelclslnetgriprglqsllqgltkgcgLQELDLSDNAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 769 TDVGARYVTKILdECKGLTHLKLGKNKITSEGGKYLALAVKNSK-SISEVGLASNGISTEGGKSLARALQQNTSLEILWL 847
Cdd:cd00116   94 GPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNL 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767944762 848 TQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLI 908
Cdd:cd00116  173 ANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL 233
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-92 3.08e-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: 74.52  E-value: 3.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767944762   21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE 73
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-868 6.19e-16

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: 79.71  E-value: 6.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 728 SRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALA 807
Cdd:cd00116  165 RDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767944762 808 VKN-SKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQ 868
Cdd:cd00116  245 LLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPG 306
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-909 4.50e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.36  E-value: 4.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGAryvtkILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886  135 LTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPE-----ELGNLTNLKELDLSNNQITD-----LPE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 807 AVKNSKSISEVGLASNGISteggkSLARALQQNTSLEILWLTQNELNDevAESLAEMLKvnqtLKHLWLIQNQITAkgta 886
Cdd:COG4886  200 PLGNLTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD--LPELGNLTN----LEELDLSNNQLTD---- 264

                        170       180
                 ....*....|....*....|...
gi 767944762 887 qlADALQSNTGITEICLNGNLIK 909
Cdd:COG4886  265 --LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-909 1.59e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 70.35  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 727 FSRLTVLRLSVNqitdggvkvlsEELTKYKIVTYLGLYNNQITDVGARyvtkiLDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886   95 LTNLTELDLSGN-----------EELSNLTNLESLDLSGNQLTDLPEE-----LANLTNLKELDLSNNQLTD-----LPE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 807 AVKNSKSISEVGLASNGISteggkSLARALQQNTSLEILWLTQNELNDevaesLAEMLKVNQTLKHLWLIQNQITAkgta 886
Cdd:COG4886  154 PLGNLTNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD---- 219

                        170       180
                 ....*....|....*....|...
gi 767944762 887 qLADALQSNTGITEICLNGNLIK 909
Cdd:COG4886  220 -LPEPLANLTNLETLDLSNNQLT 241
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 23-92 1.25e-11

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: 60.99  E-value: 1.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  23 LKSNRELLVTHIrNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:cd01671    1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRE 69
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 2.01e-11

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 61.92  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762  517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767944762  597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
718-908 1.07e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.95  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 718 YGVRELQPCFSR---LTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGaryvtKILDECKGLTHLKLGKN 794
Cdd:COG4886  146 NQLTDLPEPLGNltnLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLP-----EPLGNLTNLEELDLSGN 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 795 KITSeggkyLALAVKNSKSISEVGLASNGISTeggkslARALQQNTSLEILWLTQNELNDevAESLAEMlkvnQTLKHLW 874
Cdd:COG4886  216 QLTD-----LPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTD--LPPLANL----TNLKTLD 278

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767944762 875 LIQNQITAKGTAQLADALQSNTGITEICLNGNLI 908
Cdd:COG4886  279 LSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-914 1.29e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGaryvtKILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886  158 LTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLP-----EPLGNLTNLEELDLSGNQLTD-----LPE 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 807 AVKNSKSISEVGLASNGIST----EGGKSLAR------------ALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTL 870
Cdd:COG4886  223 PLANLTNLETLDLSNNQLTDlpelGNLTNLEEldlsnnqltdlpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLL 302

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767944762 871 KHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAK 914
Cdd:COG4886  303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 458-515 4.06e-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: 4.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767944762  458 DTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELgPGGDQQSYEF 515
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-897 4.44e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 727 FSRLTVLRLSVNQITDggVKVLSEeLTKykiVTYLGLYNNQITDVGAryvtkiLDECKGLTHLKLGKNKITSEGGKYLAL 806
Cdd:COG4886  227 LTNLETLDLSNNQLTD--LPELGN-LTN---LEELDLSNNQLTDLPP------LANLTNLKTLDLSNNQLTDLKLKELEL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944762 807 AVKNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTA 886
Cdd:COG4886  295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGL 374

                        170
                 ....*....|.
gi 767944762 887 QLADALQSNTG 897
Cdd:COG4886  375 LEATLLTLALL 385
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
 21-91 1.87e-04

Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. 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: 176764  Cd Length: 87  Bit Score: 41.06  E-value: 1.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767944762  21 QLLKSNRELLV---THIRNTQCLvDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQ 91
Cdd:cd08786    1 QWIASKREEIVsqmTEACLNQSL-DALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQKLK 73
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 23-95 1.06e-03

Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 260056  Cd Length: 81  Bit Score: 38.61  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767944762  23 LKSNRELLVTHIR-NTQCLVDNLLKNDYFSAEDA-EIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLAD 95
Cdd:cd08788    1 LQTQRPALVRRLRdHVDGALELLLTRGFFSQYDCdEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPE 75
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 20-97 4.44e-03

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: 37.42  E-value: 4.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767944762  20 IQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQlADAY 97
Cdd:cd08329    8 LSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKE-IDVV 84
 
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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