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Conserved domains on  [gi|1907197541|ref|XP_036010820|]
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NLR family, pyrin domain containing 4G isoform X3 [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 ...
 148-317 5.68e-35

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: 130.89  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 148 HMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQnKFSYTFYFCCRDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 223 EKLLFIIDSLEGMECDLtkqeselcDNCMEKQPVSILLSSLLTRKMLPESSFLLSTTPETFEKMEDRILCTDVKTATAFD 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1907197541 303 ERSIKIYFHRLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 1.40e-32

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260032  Cd Length: 84  Bit Score: 120.81  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541  10 LMWYLKELNKKEFIKFKEFLIQEILKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTERATE 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ...
gi 1907197541  90 EIA 92
Cdd:cd08320    81 EMN 83
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 552-840 3.76e-22

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 98.20  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 552 FCCLSEI-EDEAFLVKVMNCMQQINFVAKNYSDLILAAYC--LKHCSTLKKLSFSTQNV-LNEKGNQRCMKKLIICWN-- 625
Cdd:cd00116     5 LKGELLKtERATELLPKLLCLQVLRLEGNTLGEEAAKALAsaLRPQPSLKELCLSLNETgRIPRGLQSLLQGLTKGCGlq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 626 -----------DMCSVF---VRSKDIQVLQIKDTSFNEPAIRILYEYLKYPSFTLNKLVA--NNVHFFGDNHAFFELIQN 689
Cdd:cd00116    85 eldlsdnalgpDGCGVLeslLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLgrNRLEGASCEALAKALRAN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 690 CSLQYLDLGCSFLTHSEVKLLCDVLnQAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCR 769
Cdd:cd00116   165 RDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907197541 770 ALTLPYCALKSLYLNNCQITARGCQDLAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIKHPNCHLEDLRL 840
Cdd:cd00116   244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
124-486 1.69e-14

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.92  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 124 EIFI-QNDCDTFENLLISKGTEKKPHMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQNKFsYTFYFCCRDVKqlKTASLAE 202
Cdd:COG5635   156 DLYVpLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLED 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 203 LISREW----PSPSAPIEEILSQPeKLLFIIDSLEgmECDLTKQESELCDNcmekqpvsilLSSLLTRkmLPESSFLLST 278
Cdd:COG5635   233 LLAEALekrgGEPEDALERLLRNG-RLLLLLDGLD--EVPDEADRDEVLNQ----------LRRFLER--YPKARVIITS 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 279 TPETFEKMEDRILcTDVKTAtAFDERSIKIYFHRLFQDKIRAQEAF-SLVRENEQLFTICQVPLLCWMVAtclkEEIEKG 357
Cdd:COG5635   298 RPEGYDSSELEGF-EVLELA-PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLA----LLLRER 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 358 GD-PvsvcRHITSLYTTHILNLFIPQSAQ-----YPSKKSQDQLQGLCSLAAEGMWTDTFVFGEEALRR------NGILD 425
Cdd:COG5635   372 GElP----DTRAELYEQFVELLLERWDEQrgltiYRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKD 447

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907197541 426 SDI---PTLLDIGMLgkIREFENYYIFLHPSVQEVCAA----------IFYLLKSHVDhpsqDVKSIETVLFMF 486
Cdd:COG5635   448 AEAlldELLLRTGLL--VERGEGRYSFAHRSFQEYLAAralveeldeeLLELLAEHLE----DPRWREVLLLLA 515
NLRC4_HD2 super family cl39284
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 1.36e-13

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: 68.09  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 451 HPSVQEVCAAIFYLLKSHVDHP--------SQDVKSIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLVVFFGRRLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907197541 523 QKIQHKLYQCLETISgNAELQEQiDGMKLFCCLSEIEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLI-QKELSSE-RFLNLFHCLYELQDESFV 120
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-317 5.68e-35

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: 130.89  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 148 HMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQnKFSYTFYFCCRDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 223 EKLLFIIDSLEGMECDLtkqeselcDNCMEKQPVSILLSSLLTRKMLPESSFLLSTTPETFEKMEDRILCTDVKTATAFD 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1907197541 303 ERSIKIYFHRLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 1.40e-32

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 120.81  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541  10 LMWYLKELNKKEFIKFKEFLIQEILKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTERATE 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ...
gi 1907197541  90 EIA 92
Cdd:cd08320    81 EMN 83
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 1.18e-24

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 98.04  E-value: 1.18e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907197541   9 GLMWYLKELNKKEFIKFKEFLIQEIlKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 552-840 3.76e-22

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: 98.20  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 552 FCCLSEI-EDEAFLVKVMNCMQQINFVAKNYSDLILAAYC--LKHCSTLKKLSFSTQNV-LNEKGNQRCMKKLIICWN-- 625
Cdd:cd00116     5 LKGELLKtERATELLPKLLCLQVLRLEGNTLGEEAAKALAsaLRPQPSLKELCLSLNETgRIPRGLQSLLQGLTKGCGlq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 626 -----------DMCSVF---VRSKDIQVLQIKDTSFNEPAIRILYEYLKYPSFTLNKLVA--NNVHFFGDNHAFFELIQN 689
Cdd:cd00116    85 eldlsdnalgpDGCGVLeslLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLgrNRLEGASCEALAKALRAN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 690 CSLQYLDLGCSFLTHSEVKLLCDVLnQAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCR 769
Cdd:cd00116   165 RDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907197541 770 ALTLPYCALKSLYLNNCQITARGCQDLAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIKHPNCHLEDLRL 840
Cdd:cd00116   244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 645-840 4.18e-19

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: 91.00  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 645 TSFNEPAIRILYEYL--KYPSFTLNKLVANNVHFFGDNHAffelIQNCSLQYLDLGCSFLTHSEVKLLCDVLNQaECNIE 722
Cdd:COG5238   137 LPRRINLIQVLKDPLggNAVHLLGLAARLGLLAAISMAKA----LQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVT 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 723 KLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCRALTLPYcALKSLYLNNCQITARGCQDLAKVLRN 802
Cdd:COG5238   212 TLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQG 290

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907197541 803 NQNLKCLHISNNKLKDAGLMLLCKAIKHpNCHLEDLRL 840
Cdd:COG5238   291 NTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNL 327
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
124-486 1.69e-14

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.92  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 124 EIFI-QNDCDTFENLLISKGTEKKPHMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQNKFsYTFYFCCRDVKqlKTASLAE 202
Cdd:COG5635   156 DLYVpLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLED 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 203 LISREW----PSPSAPIEEILSQPeKLLFIIDSLEgmECDLTKQESELCDNcmekqpvsilLSSLLTRkmLPESSFLLST 278
Cdd:COG5635   233 LLAEALekrgGEPEDALERLLRNG-RLLLLLDGLD--EVPDEADRDEVLNQ----------LRRFLER--YPKARVIITS 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 279 TPETFEKMEDRILcTDVKTAtAFDERSIKIYFHRLFQDKIRAQEAF-SLVRENEQLFTICQVPLLCWMVAtclkEEIEKG 357
Cdd:COG5635   298 RPEGYDSSELEGF-EVLELA-PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLA----LLLRER 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 358 GD-PvsvcRHITSLYTTHILNLFIPQSAQ-----YPSKKSQDQLQGLCSLAAEGMWTDTFVFGEEALRR------NGILD 425
Cdd:COG5635   372 GElP----DTRAELYEQFVELLLERWDEQrgltiYRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKD 447

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907197541 426 SDI---PTLLDIGMLgkIREFENYYIFLHPSVQEVCAA----------IFYLLKSHVDhpsqDVKSIETVLFMF 486
Cdd:COG5635   448 AEAlldELLLRTGLL--VERGEGRYSFAHRSFQEYLAAralveeldeeLLELLAEHLE----DPRWREVLLLLA 515
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 1.36e-13

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: 68.09  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 451 HPSVQEVCAAIFYLLKSHVDHP--------SQDVKSIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLVVFFGRRLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907197541 523 QKIQHKLYQCLETISgNAELQEQiDGMKLFCCLSEIEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLI-QKELSSE-RFLNLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 8.22e-10

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: 55.26  E-value: 8.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907197541 393 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGILDSDIPTLLDIGMLGKIREFENYYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
803-830 3.38e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.46  E-value: 3.38e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907197541  803 NQNLKCLHISNNKLKDAGLMLLCKAIKH 830
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 ...
 148-317 5.68e-35

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: 130.89  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 148 HMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQnKFSYTFYFCCRDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 223 EKLLFIIDSLEGMECDLtkqeselcDNCMEKQPVSILLSSLLTRKMLPESSFLLSTTPETFEKMEDRILCTDVKTATAFD 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1907197541 303 ERSIKIYFHRLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 1.40e-32

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 120.81  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541  10 LMWYLKELNKKEFIKFKEFLIQEILKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTERATE 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ...
gi 1907197541  90 EIA 92
Cdd:cd08320    81 EMN 83
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 1.18e-24

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 98.04  E-value: 1.18e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907197541   9 GLMWYLKELNKKEFIKFKEFLIQEIlKLKLKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 552-840 3.76e-22

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: 98.20  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 552 FCCLSEI-EDEAFLVKVMNCMQQINFVAKNYSDLILAAYC--LKHCSTLKKLSFSTQNV-LNEKGNQRCMKKLIICWN-- 625
Cdd:cd00116     5 LKGELLKtERATELLPKLLCLQVLRLEGNTLGEEAAKALAsaLRPQPSLKELCLSLNETgRIPRGLQSLLQGLTKGCGlq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 626 -----------DMCSVF---VRSKDIQVLQIKDTSFNEPAIRILYEYLKYPSFTLNKLVA--NNVHFFGDNHAFFELIQN 689
Cdd:cd00116    85 eldlsdnalgpDGCGVLeslLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLgrNRLEGASCEALAKALRAN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 690 CSLQYLDLGCSFLTHSEVKLLCDVLnQAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCR 769
Cdd:cd00116   165 RDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907197541 770 ALTLPYCALKSLYLNNCQITARGCQDLAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIKHPNCHLEDLRL 840
Cdd:cd00116   244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 691-841 6.53e-22

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: 97.43  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 691 SLQYLDLGCSFLTHSE--VKLLCDVLnQAECNIEKLVLANCSLS-EQCWDYlsEVLRQNKTLSHLDISSNDLKDKGLKIL 767
Cdd:cd00116    52 SLKELCLSLNETGRIPrgLQSLLQGL-TKGCGLQELDLSDNALGpDGCGVL--ESLLRSSSLQELKLNNNGLGDRGLRLL 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907197541 768 CRALTLPYCALKSLYLNNCQITARGCQDLAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIKHpNCHLEDLRLW 841
Cdd:cd00116   129 AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLN 201
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 645-840 4.18e-19

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: 91.00  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 645 TSFNEPAIRILYEYL--KYPSFTLNKLVANNVHFFGDNHAffelIQNCSLQYLDLGCSFLTHSEVKLLCDVLNQaECNIE 722
Cdd:COG5238   137 LPRRINLIQVLKDPLggNAVHLLGLAARLGLLAAISMAKA----LQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVT 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 723 KLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCRALTLPYcALKSLYLNNCQITARGCQDLAKVLRN 802
Cdd:COG5238   212 TLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQG 290

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907197541 803 NQNLKCLHISNNKLKDAGLMLLCKAIKHpNCHLEDLRL 840
Cdd:COG5238   291 NTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNL 327
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 640-840 2.55e-15

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: 79.06  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 640 LQIKDTSFNEPAIRILYEYLK-YPSFTLNKLVANNVhffGDN--HAFFE-LIQNCSLQYLDLGCSFLTHSEVKLLCDVLn 715
Cdd:COG5238   213 LWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQI---GDEgvIALAEaLKNNTTVETLYLSGNQIGAEGAIALAKAL- 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 716 QAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCRALTLPYcALKSLYLNNCQITARGCQD 795
Cdd:COG5238   289 QGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT-TLHSLDLSDNQIGDEGAIA 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907197541 796 LAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIKHPNCHLEDLRL 840
Cdd:COG5238   368 LAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDG 412
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 686-844 4.30e-15

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: 78.68  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 686 LIQNCSLQYLDLGCSFLTHSEVKLLCDVLnQAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLK 765
Cdd:COG5238   232 LKGNKSLTTLDLSNNQIGDEGVIALAEAL-KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAI 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 766 ILCRAL--TLPycaLKSLYLNNCQITARGCQDLAKVLRNNQNLKCLHISNNKLKDAGLMLLCKAIK-HPNCHLEDLR-LW 841
Cdd:COG5238   311 ALAEGLqgNKT---LHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEgNTTLRELNLGkNN 387


                  ...
gi 1907197541 842 ITD 844
Cdd:COG5238   388 IGK 390
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
124-486 1.69e-14

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.92  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 124 EIFI-QNDCDTFENLLISKGTEKKPHMVFLQGMAGIGKTMMLKNLMLAWSKGLVFQNKFsYTFYFCCRDVKqlKTASLAE 202
Cdd:COG5635   156 DLYVpLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLED 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 203 LISREW----PSPSAPIEEILSQPeKLLFIIDSLEgmECDLTKQESELCDNcmekqpvsilLSSLLTRkmLPESSFLLST 278
Cdd:COG5635   233 LLAEALekrgGEPEDALERLLRNG-RLLLLLDGLD--EVPDEADRDEVLNQ----------LRRFLER--YPKARVIITS 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 279 TPETFEKMEDRILcTDVKTAtAFDERSIKIYFHRLFQDKIRAQEAF-SLVRENEQLFTICQVPLLCWMVAtclkEEIEKG 357
Cdd:COG5635   298 RPEGYDSSELEGF-EVLELA-PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLA----LLLRER 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 358 GD-PvsvcRHITSLYTTHILNLFIPQSAQ-----YPSKKSQDQLQGLCSLAAEGMWTDTFVFGEEALRR------NGILD 425
Cdd:COG5635   372 GElP----DTRAELYEQFVELLLERWDEQrgltiYRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKD 447

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907197541 426 SDI---PTLLDIGMLgkIREFENYYIFLHPSVQEVCAA----------IFYLLKSHVDhpsqDVKSIETVLFMF 486
Cdd:COG5635   448 AEAlldELLLRTGLL--VERGEGRYSFAHRSFQEYLAAralveeldeeLLELLAEHLE----DPRWREVLLLLA 515
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 1.36e-13

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: 68.09  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 451 HPSVQEVCAAIFYLLKSHVDHP--------SQDVKSIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLVVFFGRRLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907197541 523 QKIQHKLYQCLETISgNAELQEQiDGMKLFCCLSEIEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLI-QKELSSE-RFLNLFHCLYELQDESFV 120
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-86 2.33e-11

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. 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 CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 60.23  E-value: 2.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907197541  10 LMWYLKELNKKEFIKFKEFLIQEILKLKlKQISWTEVKKASREDLANLLLKCYEENQAWDMTFNILQKINRKDLTER 86
Cdd:cd08321     4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 8.22e-10

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: 55.26  E-value: 8.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907197541 393 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGILDSDIPTLLDIGMLGKIREFENYYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 626-788 1.38e-07

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: 54.28  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 626 DMCSVFVRSKDIQVLQIKDTSFNEPAIRILYEYLKYPSfTLNKLVANNVHFFGDNHAFFE--LIQNCSLQYLDLGCSFLT 703
Cdd:cd00116   156 ALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANC-NLEVLDLNNNGLTDEGASALAetLASLKSLEVLNLGDNNLT 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 704 HSEVKLLCDVLNQAECNIEKLVLANCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDKGLKILCRALTLPYCALKSLYL 783
Cdd:cd00116   235 DAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314


                  ....*
gi 1907197541 784 NNCQI 788
Cdd:cd00116   315 KDDSF 319
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
685-818 1.80e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.55  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 685 ELIQNCSLQYLDLGCSFLTHsevklLCDVLNQAEcNIEKLVLANCSLSEqcwdyLSEVLRQNKTLSHLDISSNDLKDkgL 764
Cdd:COG4886   108 ELSNLTNLESLDLSGNQLTD-----LPEELANLT-NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD--L 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907197541 765 KILCRALTlpycALKSLYLNNCQITargcqDLAKVLRNNQNLKCLHISNNKLKD 818
Cdd:COG4886   175 PEELGNLT----NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTD 219
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
720-818 9.66e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 9.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 720 NIEKLVLANCSLSEqcwdyLSEVLRQNKTLSHLDISSNDLKDKGLKIlcRALTlpycALKSLYLNNCQITargcqDLAKv 799
Cdd:COG4886   183 NLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLT----NLETLDLSNNQLT-----DLPE- 245

                          90
                  ....*....|....*....
gi 1907197541 800 LRNNQNLKCLHISNNKLKD 818
Cdd:COG4886   246 LGNLTNLEELDLSNNQLTD 264
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
720-824 4.26e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907197541 720 NIEKLVLANCSLSEqcwdyLSEVLRQNKTLSHLDISSNDLKDkgLKILCRaLTlpycALKSLYLNNCQITargcqDLAKv 799
Cdd:COG4886   206 NLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTD--LPELGN-LT----NLEELDLSNNQLT-----DLPP- 267

                          90       100
                  ....*....|....*....|....*
gi 1907197541 800 LRNNQNLKCLHISNNKLKDAGLMLL 824
Cdd:COG4886   268 LANLTNLKTLDLSNNQLTDLKLKEL 292
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-87 4.05e-04

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. 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 Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 39.60  E-value: 4.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907197541  10 LMWYLKELNKKEFIKFKEFLIQEILKLKLKQISWTevkkasREDLANLLLKCYEENQAWDMTFNILQKINRKDLTERA 87
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYD------RIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQL 72
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
803-830 3.38e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.46  E-value: 3.38e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907197541  803 NQNLKCLHISNNKLKDAGLMLLCKAIKH 830
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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