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Conserved domains on  [gi|767990355|ref|XP_011521562|]
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nucleotide-binding oligomerization domain-containing protein 2 isoform X6 [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 ...
 266-436 2.17e-43

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: 154.39  E-value: 2.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  266 DTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPD 345
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  346 RVLLTFDGFDEFKFRFtdrerhCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAfLRKYIRTE--FNLKGFSEQ 423
Cdd:pfam05729  81 RLLLILDGLDELVSDL------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRD-LRRGLEEPryLEVRGFSES 153

                         170
                  ....*....|...
gi 767990355  424 GIELYLRKRHHEP 436
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
CARD_NOD2_1_CARD15 cd08787
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ...
 7-92 3.97e-43

Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. 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: 176765  Cd Length: 87  Bit Score: 150.84  E-value: 3.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355   7 FQAQRSQLVELLVSG-SLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQA 85
Cdd:cd08787    1 FLAQRSELLEVLCSGgSLEPFESVLDWLLSQEVLSWEDYEGFHVLGQPLSHNARQLLDTVYNKGEWACQKFLAAAQQALA 80


                 ....*..
gi 767990355  86 DSQSPKL 92
Cdd:cd08787   81 EEQSAGL 87
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 107-187 1.07e-39

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: 141.08  E-value: 1.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 107 LQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALP 186
Cdd:cd08788    1 LQTQRPALVRRLRDHVDGALELLLTRGFFSQYDCDEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPEPPSPL 80


                 .
gi 767990355 187 L 187
Cdd:cd08788   81 N 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
96-604 8.88e-21

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 97.95  E-value: 8.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  96 WDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQH 175
Cdd:COG5635   18 LDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 176 VQELPVPLALPLEAATCKKymakLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELF 255
Cdd:COG5635   98 LLLAEALLALLELAALLKA----VLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 256 STpghLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLqcmAKPLSVRTLLFEHCCWPDVGQED 335
Cdd:COG5635  174 EL---LEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDL---AEEASLEDLLAEALEKRGGEPED 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 336 IFQLLLDHpDRVLLTFDGFDEFKFRfTDRERhcsptdptsVQTLLFNLLQGnlLKNARKVVTSRPAAV-SAFLRKYirTE 414
Cdd:COG5635  248 ALERLLRN-GRLLLLLDGLDEVPDE-ADRDE---------VLNQLRRFLER--YPKARVIITSRPEGYdSSELEGF--EV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 415 FNLKGFSEQGIELYLRKRH-HEPGVADRLIRLLQETSALHGLCHLPVFSWMVSkchqeLLLQEGGS-PKTTTDMYLLILQ 492
Cdd:COG5635  313 LELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA-----LLLRERGElPDTRAELYEQFVE 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 493 HFLlhATPPDSASQGLGPSLLRGRLPTLlhLGRLALWGLGMCCYVFSAQQLQ-------AAQVSPDDI------SLGFLV 559
Cdd:COG5635  388 LLL--ERWDEQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEeilreylGRRKDAEALldelllRTGLLV 463

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 767990355 560 -RAKGVVpgstaplEFLHITFQCFFAAFYLA--LSADVPPALLRHLFN 604
Cdd:COG5635  464 eRGEGRY-------SFAHRSFQEYLAARALVeeLDEELLELLAEHLED 504
NLRC4_HD2 super family cl39284
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 576-730 3.33e-14

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: 69.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  576 HITFQCFFAAFYLALSADV-PPALLRHLFNCGRpgnspmarllptmciqaSEGKDSSVAALLQKAEPHnLQITAAFLAGL 654
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEeKSNPLKEFFGLRK-----------------RESLKSLLDKALKSKNGH-LDLFLRFLFGL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990355  655 LSREHWGLLAECQTSEKALLRRQAcARWCLARSLRKHFHSippaapgeaksvhamPGFIWLIRSLYEMQEERLARK 730
Cdd:pfam17776  63 LNEENQRLLEGLLGCKLSSEIKQE-LLQWIKSLIQKELSS---------------ERFLNLFHCLYELQDESFVKE 122
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 266-436 2.17e-43

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: 154.39  E-value: 2.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  266 DTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPD 345
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  346 RVLLTFDGFDEFKFRFtdrerhCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAfLRKYIRTE--FNLKGFSEQ 423
Cdd:pfam05729  81 RLLLILDGLDELVSDL------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRD-LRRGLEEPryLEVRGFSES 153

                         170
                  ....*....|...
gi 767990355  424 GIELYLRKRHHEP 436
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
CARD_NOD2_1_CARD15 cd08787
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ...
 7-92 3.97e-43

Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. 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: 176765  Cd Length: 87  Bit Score: 150.84  E-value: 3.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355   7 FQAQRSQLVELLVSG-SLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQA 85
Cdd:cd08787    1 FLAQRSELLEVLCSGgSLEPFESVLDWLLSQEVLSWEDYEGFHVLGQPLSHNARQLLDTVYNKGEWACQKFLAAAQQALA 80


                 ....*..
gi 767990355  86 DSQSPKL 92
Cdd:cd08787   81 EEQSAGL 87
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 107-187 1.07e-39

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: 141.08  E-value: 1.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 107 LQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALP 186
Cdd:cd08788    1 LQTQRPALVRRLRDHVDGALELLLTRGFFSQYDCDEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPEPPSPL 80


                 .
gi 767990355 187 L 187
Cdd:cd08788   81 N 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
96-604 8.88e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 97.95  E-value: 8.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  96 WDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQH 175
Cdd:COG5635   18 LDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 176 VQELPVPLALPLEAATCKKymakLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELF 255
Cdd:COG5635   98 LLLAEALLALLELAALLKA----VLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 256 STpghLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLqcmAKPLSVRTLLFEHCCWPDVGQED 335
Cdd:COG5635  174 EL---LEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDL---AEEASLEDLLAEALEKRGGEPED 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 336 IFQLLLDHpDRVLLTFDGFDEFKFRfTDRERhcsptdptsVQTLLFNLLQGnlLKNARKVVTSRPAAV-SAFLRKYirTE 414
Cdd:COG5635  248 ALERLLRN-GRLLLLLDGLDEVPDE-ADRDE---------VLNQLRRFLER--YPKARVIITSRPEGYdSSELEGF--EV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 415 FNLKGFSEQGIELYLRKRH-HEPGVADRLIRLLQETSALHGLCHLPVFSWMVSkchqeLLLQEGGS-PKTTTDMYLLILQ 492
Cdd:COG5635  313 LELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA-----LLLRERGElPDTRAELYEQFVE 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 493 HFLlhATPPDSASQGLGPSLLRGRLPTLlhLGRLALWGLGMCCYVFSAQQLQ-------AAQVSPDDI------SLGFLV 559
Cdd:COG5635  388 LLL--ERWDEQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEeilreylGRRKDAEALldelllRTGLLV 463

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 767990355 560 -RAKGVVpgstaplEFLHITFQCFFAAFYLA--LSADVPPALLRHLFN 604
Cdd:COG5635  464 eRGEGRY-------SFAHRSFQEYLAARALVeeLDEELLELLAEHLED 504
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 4-94 2.23e-14

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: 69.13  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355    4 QEAFQAQRSQLVELLvsGSLEGfesVLDWLLSWEVLSWEDYEGFHLLGQPLSHlARRLLDTVWNKGTWACQKLIAAAQEA 83
Cdd:pfam00619   1 RKLLKKNRVALVERL--GTLDG---LLDYLLEKNVLTEEEEEKIKANPTRLDK-ARELLDLVLKKGPKACQIFLEALKEG 74

                          90
                  ....*....|.
gi 767990355   84 QADSQSPKLHG 94
Cdd:pfam00619  75 DPDLASDLEGL 85
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 576-730 3.33e-14

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: 69.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  576 HITFQCFFAAFYLALSADV-PPALLRHLFNCGRpgnspmarllptmciqaSEGKDSSVAALLQKAEPHnLQITAAFLAGL 654
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEeKSNPLKEFFGLRK-----------------RESLKSLLDKALKSKNGH-LDLFLRFLFGL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990355  655 LSREHWGLLAECQTSEKALLRRQAcARWCLARSLRKHFHSippaapgeaksvhamPGFIWLIRSLYEMQEERLARK 730
Cdd:pfam17776  63 LNEENQRLLEGLLGCKLSSEIKQE-LLQWIKSLIQKELSS---------------ERFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 519-574 5.27e-08

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: 49.87  E-value: 5.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767990355  519 TLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLEF 574
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 267-366 3.19e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355   267 TVLVVGEAGSGKSTLLQRLhllwaAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQ--EDIFQLLLDHP 344
Cdd:smart00382   4 VILIVGPPGSGKTTLARAL-----ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 767990355   345 DRVLLtfdgFDEFkFRFTDRER 366
Cdd:smart00382  79 PDVLI----LDEI-TSLLDAEQ 95
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 107-188 6.11e-03

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: 36.38  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  107 LQSHRPAIVRRLHShVENMLDLAWERGFVSQYECDEIRLPIFTPSQrARRLLDLATVKANGLAAFLLQHVQELPVPLALP 186
Cdd:pfam00619   4 LKKNRVALVERLGT-LDGLLDYLLEKNVLTEEEEEKIKANPTRLDK-ARELLDLVLKKGPKACQIFLEALKEGDPDLASD 81


                  ..
gi 767990355  187 LE 188
Cdd:pfam00619  82 LE 83
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 266-436 2.17e-43

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: 154.39  E-value: 2.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  266 DTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPD 345
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  346 RVLLTFDGFDEFKFRFtdrerhCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAfLRKYIRTE--FNLKGFSEQ 423
Cdd:pfam05729  81 RLLLILDGLDELVSDL------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRD-LRRGLEEPryLEVRGFSES 153

                         170
                  ....*....|...
gi 767990355  424 GIELYLRKRHHEP 436
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
CARD_NOD2_1_CARD15 cd08787
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ...
 7-92 3.97e-43

Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. 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: 176765  Cd Length: 87  Bit Score: 150.84  E-value: 3.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355   7 FQAQRSQLVELLVSG-SLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQA 85
Cdd:cd08787    1 FLAQRSELLEVLCSGgSLEPFESVLDWLLSQEVLSWEDYEGFHVLGQPLSHNARQLLDTVYNKGEWACQKFLAAAQQALA 80


                 ....*..
gi 767990355  86 DSQSPKL 92
Cdd:cd08787   81 EEQSAGL 87
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 107-187 1.07e-39

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: 141.08  E-value: 1.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 107 LQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALP 186
Cdd:cd08788    1 LQTQRPALVRRLRDHVDGALELLLTRGFFSQYDCDEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPEPPSPL 80


                 .
gi 767990355 187 L 187
Cdd:cd08788   81 N 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
96-604 8.88e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 97.95  E-value: 8.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  96 WDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQH 175
Cdd:COG5635   18 LDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 176 VQELPVPLALPLEAATCKKymakLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELF 255
Cdd:COG5635   98 LLLAEALLALLELAALLKA----VLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 256 STpghLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLqcmAKPLSVRTLLFEHCCWPDVGQED 335
Cdd:COG5635  174 EL---LEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDL---AEEASLEDLLAEALEKRGGEPED 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 336 IFQLLLDHpDRVLLTFDGFDEFKFRfTDRERhcsptdptsVQTLLFNLLQGnlLKNARKVVTSRPAAV-SAFLRKYirTE 414
Cdd:COG5635  248 ALERLLRN-GRLLLLLDGLDEVPDE-ADRDE---------VLNQLRRFLER--YPKARVIITSRPEGYdSSELEGF--EV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 415 FNLKGFSEQGIELYLRKRH-HEPGVADRLIRLLQETSALHGLCHLPVFSWMVSkchqeLLLQEGGS-PKTTTDMYLLILQ 492
Cdd:COG5635  313 LELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA-----LLLRERGElPDTRAELYEQFVE 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 493 HFLlhATPPDSASQGLGPSLLRGRLPTLlhLGRLALWGLGMCCYVFSAQQLQ-------AAQVSPDDI------SLGFLV 559
Cdd:COG5635  388 LLL--ERWDEQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEeilreylGRRKDAEALldelllRTGLLV 463

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 767990355 560 -RAKGVVpgstaplEFLHITFQCFFAAFYLA--LSADVPPALLRHLFN 604
Cdd:COG5635  464 eRGEGRY-------SFAHRSFQEYLAARALVeeLDEELLELLAEHLED 504
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 4-94 2.23e-14

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: 69.13  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355    4 QEAFQAQRSQLVELLvsGSLEGfesVLDWLLSWEVLSWEDYEGFHLLGQPLSHlARRLLDTVWNKGTWACQKLIAAAQEA 83
Cdd:pfam00619   1 RKLLKKNRVALVERL--GTLDG---LLDYLLEKNVLTEEEEEKIKANPTRLDK-ARELLDLVLKKGPKACQIFLEALKEG 74

                          90
                  ....*....|.
gi 767990355   84 QADSQSPKLHG 94
Cdd:pfam00619  75 DPDLASDLEGL 85
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 576-730 3.33e-14

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: 69.63  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  576 HITFQCFFAAFYLALSADV-PPALLRHLFNCGRpgnspmarllptmciqaSEGKDSSVAALLQKAEPHnLQITAAFLAGL 654
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEeKSNPLKEFFGLRK-----------------RESLKSLLDKALKSKNGH-LDLFLRFLFGL 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990355  655 LSREHWGLLAECQTSEKALLRRQAcARWCLARSLRKHFHSippaapgeaksvhamPGFIWLIRSLYEMQEERLARK 730
Cdd:pfam17776  63 LNEENQRLLEGLLGCKLSSEIKQE-LLQWIKSLIQKELSS---------------ERFLNLFHCLYELQDESFVKE 122
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 8-82 1.91e-08

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: 51.75  E-value: 1.91e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990355   8 QAQRSQLVELLVSgslegfESVLDWLLSWEVLSWEDYEGFHLLGQPlSHLARRLLDTVWNKGTWACQKLIAAAQE 82
Cdd:cd01671    2 RKNRVELVEDLDV------EDILDHLIQKGVLTEEDKEEILSEKTR-QDKARKLLDILPRRGPKAFEVFCEALRE 69
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 519-574 5.27e-08

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: 49.87  E-value: 5.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767990355  519 TLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLEF 574
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 107-187 1.08e-07

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: 49.82  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355 107 LQSHRPAIVRRLHshVENMLDLAWERGFVSQYECDEIRLPIfTPSQRARRLLDLATVKANGLAAFLLQHVQELPVP-LAL 185
Cdd:cd01671    1 LRKNRVELVEDLD--VEDILDHLIQKGVLTEEDKEEILSEK-TRQDKARKLLDILPRRGPKAFEVFCEALRETGQPhLAE 77


                 ..
gi 767990355 186 PL 187
Cdd:cd01671   78 LL 79
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 107-183 1.29e-04

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: 41.66  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990355 107 LQSHRPAIVRRLHShVENMLDLAWERGFVSQYECDEIRLPIFTPSQrARRLLDLATVKANGLAAFLLQHVQELPVPL 183
Cdd:cd08329   11 IRKNRMALFQHLTC-VLPILDHLLSANVITEQEYDVIKQKTQTPLQ-ARELIDTILVKGNAAAEVFRNCLKEIDVVL 85
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 267-366 3.19e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355   267 TVLVVGEAGSGKSTLLQRLhllwaAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQ--EDIFQLLLDHP 344
Cdd:smart00382   4 VILIVGPPGSGKTTLARAL-----ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlRLALALARKLK 78

                           90       100
                   ....*....|....*....|..
gi 767990355   345 DRVLLtfdgFDEFkFRFTDRER 366
Cdd:smart00382  79 PDVLI----LDEI-TSLLDAEQ 95
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 107-188 6.11e-03

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: 36.38  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990355  107 LQSHRPAIVRRLHShVENMLDLAWERGFVSQYECDEIRLPIFTPSQrARRLLDLATVKANGLAAFLLQHVQELPVPLALP 186
Cdd:pfam00619   4 LKKNRVALVERLGT-LDGLLDYLLEKNVLTEEEEEKIKANPTRLDK-ARELLDLVLKKGPKACQIFLEALKEGDPDLASD 81


                  ..
gi 767990355  187 LE 188
Cdd:pfam00619  82 LE 83
 
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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