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Conserved domains on  [gi|74215756|dbj|BAE23420|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-950 3.70e-45

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: 168.82  E-value: 3.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 730 LTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 810 NSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74215756 890 EMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.79e-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: 156.70  E-value: 5.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 74215756   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 8.32e-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: 144.54  E-value: 8.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                ....
gi 74215756 101 RLWL 104
Cdd:cd08324  81 RPWL 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 2.00e-21

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635 250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635 383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 74215756 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 1.52e-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: 59.61  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74215756   597 AKARQKLLRQLVPKAILRRKRKalwahlfaSLRSYLKSLPRvqsGGFNQVHamptFLWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQ---KELSSER----FLNLFHCLYELQDE 117
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-950 3.70e-45

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: 168.82  E-value: 3.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 730 LTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 810 NSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74215756 890 EMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.79e-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: 156.70  E-value: 5.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 74215756   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 8.32e-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: 144.54  E-value: 8.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                ....
gi 74215756 101 RLWL 104
Cdd:cd08324  81 RPWL 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-941 1.31e-23

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: 102.82  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 728 SRLTVIRLSVNQITDTGVKVLcEELTKYKIVTFLGLYNNQITDIGARYVAQILDECR-GLKHLKLGKNRITSEGGKCVAL 806
Cdd:cd00116  81 CGLQELDLSDNALGPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAK 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 807 AVKNSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAE 886
Cdd:cd00116 160 ALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAA 239

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74215756 887 CFAE-MLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEA 941
Cdd:cd00116 240 ALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 2.00e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635 250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635 383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 74215756 494 LQLGFLRalpdvgPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLR 542
Cdd:COG5635 457 LRTGLLV------ERGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-105 5.22e-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: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756    21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQlEDAYVDL 100
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLAS 80


                  ....*
gi 74215756   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 1.52e-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: 59.61  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74215756   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 3.38e-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: 3.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74215756   460 TLHALGEVAHRGTDKSLFVFGQEEVQASKLQEGDLQLGFLRALPDVGPEQGQSYEF 515
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
839-866 9.85e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.31  E-value: 9.85e-03
                           10        20
                   ....*....|....*....|....*...
gi 74215756    839 HPSLTTLSLAFNGISPEGGKSLAQALKQ 866
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-950 3.70e-45

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: 168.82  E-value: 3.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 730 LTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 810 NSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74215756 890 EMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEIcLNGNLIKPE-EAKVFENEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLI-LDGNLIGAEaQQRLEQLLERI 430
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 197-367 5.79e-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: 156.70  E-value: 5.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   197 TVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESdmLSLQDLLFKHFCYPEQDPEEVFSFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   277 HTALFTFDGLDELHSDFDLSRVPDSccpwepahPLVLLANLLSGRLLKGAGKLLTARTG--VEVPRQLLRKKVL-LRGFS 353
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDalRDLRRGLEEPRYLeVRGFS 151

                         170
                  ....*....|....
gi 74215756   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 8.32e-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: 144.54  E-value: 8.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756  21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80


                ....
gi 74215756 101 RLWL 104
Cdd:cd08324  81 RPWL 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-941 1.31e-23

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: 102.82  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 728 SRLTVIRLSVNQITDTGVKVLcEELTKYKIVTFLGLYNNQITDIGARYVAQILDECR-GLKHLKLGKNRITSEGGKCVAL 806
Cdd:cd00116  81 CGLQELDLSDNALGPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAK 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 807 AVKNSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAE 886
Cdd:cd00116 160 ALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAA 239

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74215756 887 CFAE-MLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEA 941
Cdd:cd00116 240 ALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
190-542 2.00e-21

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.65  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 190 VLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFScfkesDMLSLQDLLFKHFCYPEQDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA-----EEASLEDLLAEALEKRGGEPEDAL 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 270 SFLLRfPHTALFTFDGLDELHSDFDLSRVpdsccpwepahpLVLLANLLSGrlLKGAGKLLTARTgVEVPRQLLR--KKV 347
Cdd:COG5635 250 ERLLR-NGRLLLLLDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 348 LLRGFSPSHLRAYARRMFPERTAQ-EHLLQQLDANPNLCSLCGVPLFCWIIfrCFQHfqtvfeGSSSQLPDcavTLTDVF 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--ALLL------RERGELPD---TRAELY 382

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 427 LLVTEVHLNRPQPSSLVQRNTRSPAETLRAgwrtlhALGEVAHRGTDKSLFVFGQEEVQASK-------------LQEGD 493
Cdd:COG5635 383 EQFVELLLERWDEQRGLTIYRELSREELRE------LLSELALAMQENGRTEFAREELEEILreylgrrkdaealLDELL 456

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 74215756 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 ...
 723-903 1.91e-20

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 93.57  E-value: 1.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 723 LQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGK 802
Cdd:cd00116 132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 803 CVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEALK-DHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELN 881
Cdd:cd00116 212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291

                       170       180
                ....*....|....*....|...
gi 74215756 882 DESAECFAEMLRVNQ-TLRHLWL 903
Cdd:cd00116 292 EEGAQLLAESLLEPGnELESLWV 314
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 742-942 1.93e-20

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 93.19  E-value: 1.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 742 DTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILdECRGLKHLKLGKNRITSEGGKCVALAVKNSTSIVDV-GMW 820
Cdd:cd00116  67 PRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKlVLG 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 821 GNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRH 900
Cdd:cd00116 146 RNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEV 225

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 74215756 901 LWLIQNRITAKGTAQLARALQK-NTAITEICLNGNLIKPEEAK 942
Cdd:cd00116 226 LNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAK 268
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 728-920 3.26e-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: 86.64  E-value: 3.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 728 SRLTVIRLSVNQITDTGVKVLCEELTKYKI-VTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVAL 806
Cdd:cd00116 108 SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAE 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 807 AVKNSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQ-NTTLTVIWLTKNELNDESA 885
Cdd:cd00116 188 GLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGA 267

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74215756 886 ECFAEMLRVNQTLRHLWLIQNRITAKGTAQLARAL 920
Cdd:cd00116 268 KDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 21-105 5.22e-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: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756    21 KLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQlEDAYVDL 100
Cdd:pfam00619   2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE-GDPDLAS 80


                  ....*
gi 74215756   101 RLWLS 105
Cdd:pfam00619  81 DLEGL 85
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 719-945 4.94e-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: 4.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 719 GVQELQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVT--FLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNri 796
Cdd:cd00116  14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKelCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDN-- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 797 tseggkcvalavknstsivdvgmwgnQIGDEGAKAFaEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNT-TLTVIWL 875
Cdd:cd00116  92 --------------------------ALGPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVL 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 876 TKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVFE 945
Cdd:cd00116 145 GRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALA 214
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-950 3.31e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 72.66  E-value: 3.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 727 FSRLTVIRLSVNQITDtgvkvLCEELTKYKIVTFLGLYNNQITDIGARyvaqiLDECRGLKHLKLGKNRITSeggkcVAL 806
Cdd:COG4886 112 LTNLESLDLSGNQLTD-----LPEELANLTNLKELDLSNNQLTDLPEP-----LGNLTNLKSLDLSNNQLTD-----LPE 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 807 AVKNSTSIVDVGMWGNQIGDegakaFAEALKDHPSLTTLSLAFNGISpeggkSLAQALKQNTTLTVIWLTKNELNDesae 886
Cdd:COG4886 177 ELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD---- 242

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74215756 887 cFAEMLRVNQtLRHLWLIQNRITAkgtaqlARALQKNTAITEICLNGNLIKPEEAKVFENEKRI 950
Cdd:COG4886 243 -LPELGNLTN-LEELDLSNNQLTD------LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGL 298
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 23-98 2.47e-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: 2.47e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74215756  23 LKINREHLVTNIrNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYV 98
Cdd:cd01671   1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHL 75
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
727-946 7.76e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.34  E-value: 7.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 727 FSRLTVIRLSVNQITDtgvkvLCEELTKYKIVTFLGLYNNQITDIGAryvaqILDECRGLKHLKLGKNRITSeggkcVAL 806
Cdd:COG4886 158 LTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLPE-----PLGNLTNLEELDLSGNQLTD-----LPE 222

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756 807 AVKNSTSIVDVGMWGNQIGDegakafAEALKDHPSLTTLSLAFNGIS--PEggkslaqaLKQNTTLTVIWLTKNELNDES 884
Cdd:COG4886 223 PLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTdlPP--------LANLTNLKTLDLSNNQLTDLK 288

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74215756 885 AECFAEMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVFEN 946
Cdd:COG4886 289 LKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 517-665 1.52e-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: 59.61  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74215756   517 HLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFfsfqclggrsrlgpdpfRNKDHFQFTNLFLCGLL 596
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALK-----------------SKNGHLDLFLRFLFGLL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74215756   597 AKARQKLLRQLVPKAILRRKRKalwahlfaSLRSYLKSLPRvqsGGFNQVHamptFLWMLRCIYETQSQ 665
Cdd:pfam17776  64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQ---KELSSER----FLNLFHCLYELQDE 117
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
 23-95 1.80e-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: 1.80e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74215756  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 3.38e-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: 3.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74215756   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 3.08e-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: 3.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 74215756  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 3.26e-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: 37.20  E-value: 3.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74215756  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 9.13e-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: 9.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74215756    27 REHLVTNIRNTQC----------LVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQS 77
Cdd:pfam04963  13 QEHLLWQLRLSPLserdraiaeyLIGNLDEDGYLRESLEEIAEELGVSEEEVEAVLKLIQS 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
839-866 9.85e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.31  E-value: 9.85e-03
                           10        20
                   ....*....|....*....|....*...
gi 74215756    839 HPSLTTLSLAFNGISPEGGKSLAQALKQ 866
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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