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Conserved domains on  [gi|1237938045|ref|NP_001341778|]
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nucleotide-binding oligomerization domain-containing protein 1 isoform 2 [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 1237938045 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 1237938045 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 1237938045  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324     1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                  ....*
gi 1237938045 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 1237938045 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238   237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238   317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1237938045 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 1237938045 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635   175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635   250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635   314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635   384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1237938045 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 1237938045 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938045 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 1237938045 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 1237938045 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 1237938045  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324     1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                  ....*
gi 1237938045 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 1237938045 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238   237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238   317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1237938045 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 1237938045 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635   175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635   250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635   314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635   384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1237938045 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 1237938045 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116    24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGLASNGISTEG 828
Cdd:cd00116   102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 829 GKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQS-NTGITEICLNGNL 907
Cdd:cd00116   182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCND 261


                  ....*..
gi 1237938045 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 1237938045  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 1237938045 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938045 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 1237938045 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 1237938045 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 1237938045 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 1237938045  21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324     1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                  ....*
gi 1237938045 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 1237938045 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238   237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238   317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1237938045 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 1237938045 730 LTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVK 809
Cdd:COG5238   210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 810 NSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLA 889
Cdd:COG5238   290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                         170       180
                  ....*....|....*....|....*
gi 1237938045 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 1237938045 729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAV 808
Cdd:COG5238   181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 809 KNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQL 888
Cdd:COG5238   261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIAL 340

                         170       180
                  ....*....|....*....|....*..
gi 1237938045 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 1237938045 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635   175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635   250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635   314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635   384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1237938045 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 1237938045 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116    24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGLASNGISTEG 828
Cdd:cd00116   102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 829 GKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQS-NTGITEICLNGNL 907
Cdd:cd00116   182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCND 261


                  ....*..
gi 1237938045 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 1237938045 723 LQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGK 802
Cdd:cd00116   132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 803 YLALAVKNSKSISEVGLASNGISTEGGKSLARAL-QQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQIT 881
Cdd:cd00116   212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291

                         170
                  ....*....|.
gi 1237938045 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 1237938045 719 GVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKI------------------------------VTYLGLYNNQI 768
Cdd:cd00116    14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSlkelclslnetgriprglqsllqgltkgcgLQELDLSDNAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 769 TDVGARYVTKILdECKGLTHLKLGKNKITSEGGKYLALAVKNSK-SISEVGLASNGISTEGGKSLARALQQNTSLEILWL 847
Cdd:cd00116    94 GPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237938045 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 1237938045  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 1237938045 728 SRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALA 807
Cdd:cd00116   165 RDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237938045 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 1237938045 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGAryvtkILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886   135 LTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPE-----ELGNLTNLKELDLSNNQITD-----LPE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 807 AVKNSKSISEVGLASNGISteggkSLARALQQNTSLEILWLTQNELNDevAESLAEMLKvnqtLKHLWLIQNQITAkgta 886
Cdd:COG4886   200 PLGNLTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD--LPELGNLTN----LEELDLSNNQLTD---- 264

                         170       180
                  ....*....|....*....|...
gi 1237938045 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 1237938045 727 FSRLTVLRLSVNqitdggvkvlsEELTKYKIVTYLGLYNNQITDVGARyvtkiLDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886    95 LTNLTELDLSGN-----------EELSNLTNLESLDLSGNQLTDLPEE-----LANLTNLKELDLSNNQLTD-----LPE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 807 AVKNSKSISEVGLASNGISteggkSLARALQQNTSLEILWLTQNELNDevaesLAEMLKVNQTLKHLWLIQNQITAkgta 886
Cdd:COG4886   154 PLGNLTNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD---- 219

                         170       180
                  ....*....|....*....|...
gi 1237938045 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 1237938045  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 1237938045 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938045 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 1237938045 718 YGVRELQPCFSR---LTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGaryvtKILDECKGLTHLKLGKN 794
Cdd:COG4886   146 NQLTDLPEPLGNltnLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLP-----EPLGNLTNLEELDLSGN 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 795 KITSeggkyLALAVKNSKSISEVGLASNGISTeggkslARALQQNTSLEILWLTQNELNDevAESLAEMlkvnQTLKHLW 874
Cdd:COG4886   216 QLTD-----LPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTD--LPPLANL----TNLKTLD 278

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1237938045 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 1237938045 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGaryvtKILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886   158 LTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLP-----EPLGNLTNLEELDLSGNQLTD-----LPE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 807 AVKNSKSISEVGLASNGIST----EGGKSLAR------------ALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTL 870
Cdd:COG4886   223 PLANLTNLETLDLSNNQLTDlpelGNLTNLEEldlsnnqltdlpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLL 302

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1237938045 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 1237938045 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 1237938045 727 FSRLTVLRLSVNQITDggVKVLSEeLTKykiVTYLGLYNNQITDVGAryvtkiLDECKGLTHLKLGKNKITSEGGKYLAL 806
Cdd:COG4886   227 LTNLETLDLSNNQLTD--LPELGN-LTN---LEELDLSNNQLTDLPP------LANLTNLKTLDLSNNQLTDLKLKELEL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938045 807 AVKNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTA 886
Cdd:COG4886   295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGL 374

                         170
                  ....*....|.
gi 1237938045 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 1237938045  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 1237938045  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 1237938045  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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