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Conserved domains on  [gi|568940120|ref|XP_006505341|]
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nucleotide-binding oligomerization domain-containing protein 1 isoform X1 [Mus musculus]

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 8.13e-44

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: 156.31  E-value: 8.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 568940120  354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 21-104 6.05e-41

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08324:

Pssm-ID: 472698  Cd Length: 85  Bit Score: 144.93  E-value: 6.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....
gi 568940120 101 RLWL 104
Cdd:cd08324   81 RPWL 84
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.67e-40

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: 154.18  E-value: 3.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 729 RLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEAL 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 809 KDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568940120 889 ARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 922
Cdd:COG5238  397 IDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 1.93e-21

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635  250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635  383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568940120 494 LQLGFLRalpdvgPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLR 542
Cdd:COG5635  457 LRTGLLV------ERGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
NLRC4_HD2 super family cl39284
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 1.70e-10

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: 59.23  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940120  597 AKARQKLLRQLVPKAILRRKRKalwahlfaSLRSYLKSLPRvqsGGFNQVHamptFLWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQ---KELSSER----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 8.13e-44

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: 156.31  E-value: 8.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 568940120  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 ...
 21-104 6.05e-41

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: 144.93  E-value: 6.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....
gi 568940120 101 RLWL 104
Cdd:cd08324   81 RPWL 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.67e-40

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: 154.18  E-value: 3.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 729 RLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEAL 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 809 KDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568940120 889 ARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 922
Cdd:COG5238  397 IDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 1.93e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635  250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635  383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568940120 494 LQLGFLRalpdvgPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLR 542
Cdd:COG5635  457 LRTGLLV------ERGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-913 4.20e-21

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: 95.11  E-value: 4.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 728 SRLTVIRLSVNQITDTGVKVLCEELTKYKI-VTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAE 806
Cdd:cd00116  108 SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAE 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 807 ALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAE-MLRVNQTLRHLWLIQNRITAKGT 885
Cdd:cd00116  188 GLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGA 267

                        170       180
                 ....*....|....*....|....*...
gi 568940120 886 AQLARALQKNTAITEICLNGNLIKPEEA 913
Cdd:cd00116  268 KDLAEVLAEKESLLELDLRGNKFGEEGA 295
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-105 4.50e-18

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: 79.53  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120   21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQlEDAYVDL 100
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLAS 80


                  ....*
gi 568940120  101 RLWLS 105
Cdd:pfam00619  81 DLEGL 85
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 1.70e-10

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: 59.23  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940120  597 AKARQKLLRQLVPKAILRRKRKalwahlfaSLRSYLKSLPRvqsGGFNQVHamptFLWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQ---KELSSER----FLNLFHCLYELQDE 117
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 460-515 3.55e-05

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: 42.17  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940120  460 TLHALGEVAHRGTDKSLFVFGQEEVQASKLQEGDLQLGFLRALPDVGPEQGQSYEF 515
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
811-838 9.29e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 9.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 568940120   811 HPSLTTLSLAFNGISPEGGKSLAQALKQ 838
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
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 8.13e-44

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: 156.31  E-value: 8.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 568940120  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 ...
 21-104 6.05e-41

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: 144.93  E-value: 6.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324    1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                 ....
gi 568940120 101 RLWL 104
Cdd:cd08324   81 RPWL 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-922 3.67e-40

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: 154.18  E-value: 3.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 729 RLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEAL 808
Cdd:COG5238  237 SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 809 KDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQL 888
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568940120 889 ARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 922
Cdd:COG5238  397 IDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-916 2.10e-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: 149.17  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 729 RLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEAL 808
Cdd:COG5238  181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 809 KDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQL 888
Cdd:COG5238  261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIAL 340

                        170       180
                 ....*....|....*....|....*...
gi 568940120 889 ARALQKNTAITEICLNGNLIKPEEAKVF 916
Cdd:COG5238  341 AKALQENTTLHSLDLSDNQIGDEGAIAL 368
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-914 1.87e-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: 134.53  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 730 LTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEALK 809
Cdd:COG5238  210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 810 DHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQLA 889
Cdd:COG5238  290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                        170       180
                 ....*....|....*....|....*
gi 568940120 890 RALQKNTAITEICLNGNLIKPEEAK 914
Cdd:COG5238  370 KYLEGNTTLRELNLGKNNIGKQGAE 394
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 782-916 5.91e-29

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: 121.05  E-value: 5.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 782 NSTSIVDVGmwGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFA 861
Cdd:COG5238  180 NSVETVYLG--CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568940120 862 EMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVF 916
Cdd:COG5238  258 EALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIAL 312
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 1.93e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635  175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635  250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635  314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635  383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568940120 494 LQLGFLRalpdvgPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLR 542
Cdd:COG5635  457 LRTGLLV------ERGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-913 4.20e-21

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: 95.11  E-value: 4.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 728 SRLTVIRLSVNQITDTGVKVLCEELTKYKI-VTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAE 806
Cdd:cd00116  108 SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAE 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 807 ALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAE-MLRVNQTLRHLWLIQNRITAKGT 885
Cdd:cd00116  188 GLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGA 267

                        170       180
                 ....*....|....*....|....*...
gi 568940120 886 AQLARALQKNTAITEICLNGNLIKPEEA 913
Cdd:cd00116  268 KDLAEVLAEKESLLELDLRGNKFGEEGA 295
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-914 1.44e-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: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 728 SRLTVIRLSVNQITDTGVKVLcEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDV-GMWGNQIGDEGAKAFAE 806
Cdd:cd00116   81 CGLQELDLSDNALGPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKlVLGRNRLEGASCEALAK 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 807 ALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTA 886
Cdd:cd00116  160 ALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAA 239

                        170       180
                 ....*....|....*....|....*....
gi 568940120 887 QLARALQK-NTAITEICLNGNLIKPEEAK 914
Cdd:cd00116  240 ALASALLSpNISLLTLSLSCNDITDDGAK 268
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-105 4.50e-18

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: 79.53  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120   21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQlEDAYVDL 100
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLAS 80


                  ....*
gi 568940120  101 RLWLS 105
Cdd:pfam00619  81 DLEGL 85
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-875 3.62e-17

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: 83.56  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 728 SRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEA 807
Cdd:cd00116  165 RDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 808 LK-DHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQ-TLRHLWL 875
Cdd:cd00116  245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGnELESLWV 314
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 723-892 5.10e-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: 80.09  E-value: 5.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 723 LQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAK 802
Cdd:cd00116  132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 803 AFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQ-NTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRIT 881
Cdd:cd00116  212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291

                        170
                 ....*....|.
gi 568940120 882 AKGTAQLARAL 892
Cdd:cd00116  292 EEGAQLLAESL 302
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 719-917 3.53e-15

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: 77.78  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 719 GVQELQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVT--FLGLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQI 796
Cdd:cd00116   14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKelCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 797 GDEGAKAFaEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNT-TLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWL 875
Cdd:cd00116   94 GPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568940120 876 IQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVFE 917
Cdd:cd00116  173 ANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALA 214
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 725-839 3.99e-14

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: 74.31  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 725 PCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLGKNRITSEGGKCVALAVKN-STSIVDVGMWGNQIGDEGAKA 803
Cdd:cd00116  190 KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAKD 269

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568940120 804 FAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQN 839
Cdd:cd00116  270 LAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEP 305
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 23-98 2.11e-12

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: 63.30  E-value: 2.11e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940120  23 LKINREHLVTNIrNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYV 98
Cdd:cd01671    1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHL 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 1.70e-10

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: 59.23  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120  517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940120  597 AKARQKLLRQLVPKAILRRKRKalwahlfaSLRSYLKSLPRvqsGGFNQVHamptFLWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQ---KELSSER----FLNLFHCLYELQDE 117
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
749-909 2.49e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 749 CEELTKYKIVTFLGLGKNRITSeggkcVALAVKNSTSIVDVGMWGNQIGDegakaFAEALKDHPSLTTLSLAFNGISpeg 828
Cdd:COG4886  106 NEELSNLTNLESLDLSGNQLTD-----LPEELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLT--- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940120 829 gkSLAQALKQNTTLTVIWLTKNELNDesaecFAEMLRVNQTLRHLWLIQNRITAkgtaqLARALQKNTAITEICLNGNLI 908
Cdd:COG4886  173 --DLPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL 240


                 .
gi 568940120 909 K 909
Cdd:COG4886  241 T 241
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 23-95 1.85e-05

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: 43.62  E-value: 1.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940120  23 LKINREHLVTNIR-NTQCLVDNLLENGYFSAEDA-EIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLED 95
Cdd:cd08788    1 LQTQRPALVRRLRdHVDGALELLLTRGFFSQYDCdEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPE 75
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 460-515 3.55e-05

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: 42.17  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568940120  460 TLHALGEVAHRGTDKSLFVFGQEEVQASKLQEGDLQLGFLRALPDVGPEQGQSYEF 515
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
 41-91 2.85e-03

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: 37.59  E-value: 2.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568940120  41 VDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQ 91
Cdd:cd08786   23 LDALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQKLK 73
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 26-94 2.95e-03

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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: 260039  Cd Length: 81  Bit Score: 37.58  E-value: 2.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940120  26 NREHLVTNIRNTQCLVDNLLENgYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLE 94
Cdd:cd08330    6 HREALIQRVTNVDPILDELRGK-VLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETN 73
Sigma54_CBD pfam04963
Sigma-54 factor, core binding domain; This domain makes a direct interaction with the core RNA ...
 27-77 8.36e-03

Sigma-54 factor, core binding domain; This domain makes a direct interaction with the core RNA polymerase, to form an enhancer dependent holoenzyme. The centre of this domain contains a very weak similarity to a helix-turn-helix motif which may represent the other DNA binding domain.


Pssm-ID: 461501 [Multi-domain]  Cd Length: 182  Bit Score: 38.20  E-value: 8.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940120   27 REHLVTNIRNTQC----------LVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQS 77
Cdd:pfam04963  13 QEHLLWQLRLSPLserdraiaeyLIGNLDEDGYLRESLEEIAEELGVSEEEVEAVLKLIQS 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
811-838 9.29e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 9.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 568940120   811 HPSLTTLSLAFNGISPEGGKSLAQALKQ 838
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
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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