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Conserved domains on  [gi|75709196|ref|NP_996611|]
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NACHT, LRR and PYD domains-containing protein 7 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 172-340 9.67e-47

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: 164.79  E-value: 9.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 75709196   327 EDRRAYFLRHFGDE 340
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 6.60e-29

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: 110.41  E-value: 6.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196  10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 75709196  90 EMME 93
Cdd:cd08320  81 EMNE 84
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 751-940 1.14e-27

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: 114.76  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 751 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 825
Cdd:cd00116 127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 826 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 905
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75709196 906 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 940
Cdd:cd00116 281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 3.40e-23

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: 95.82  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 75709196   544 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 585
Cdd:pfam17776  81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 412-466 2.75e-12

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: 62.20  E-value: 2.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 75709196   412 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 466
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 172-340 9.67e-47

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: 164.79  E-value: 9.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 75709196   327 EDRRAYFLRHFGDE 340
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 6.60e-29

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: 110.41  E-value: 6.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196  10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 75709196  90 EMME 93
Cdd:cd08320  81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 751-940 1.14e-27

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: 114.76  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 751 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 825
Cdd:cd00116 127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 826 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 905
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75709196 906 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 940
Cdd:cd00116 281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 3.40e-23

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: 95.82  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 75709196   544 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 585
Cdd:pfam17776  81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-530 1.54e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.12  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 153 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 229
Cdd:COG5635 168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 230 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 308
Cdd:COG5635 240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 309 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 387
Cdd:COG5635 305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 388 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 452
Cdd:COG5635 376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 453 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 529
Cdd:COG5635 456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                .
gi 75709196 530 R 530
Cdd:COG5635 522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 762-970 2.82e-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: 91.78  E-value: 2.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 762 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 841
Cdd:COG5238 209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 842 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 920
Cdd:COG5238 288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75709196 921 ILCQALENpNCNLKHLRL-KTYETNLEIKKLLEEVKEKN-PKLTIDCNASGA 970
Cdd:COG5238 367 ALAKYLEG-NTTLRELNLgKNNIGKQGAEALIDALQTNRlHTLILDGNLIGA 417
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 8.47e-18

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: 78.78  E-value: 8.47e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75709196    10 LQTLLEQLNEDELKSFKSLLWAFPLEDvLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCK 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEG-LRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 412-466 2.75e-12

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: 62.20  E-value: 2.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 75709196   412 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 466
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 173-311 6.22e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196    173 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 247
Cdd:smart00382   4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75709196    248 --ILFvvdgLDElkvpPGALIQDICGDWEKKKPVPVLLGSLLKRKmlPRAALLVTTRPRALRDLQL 311
Cdd:smart00382  79 pdVLI----LDE----ITSLLDAEQEALLLLLEELRLLLLLKSEK--NLTVILTTNDEKDLGPALL 134
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 172-340 9.67e-47

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: 164.79  E-value: 9.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 75709196   327 EDRRAYFLRHFGDE 340
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 6.60e-29

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: 110.41  E-value: 6.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196  10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 75709196  90 EMME 93
Cdd:cd08320  81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 751-940 1.14e-27

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: 114.76  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 751 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 825
Cdd:cd00116 127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 826 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 905
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75709196 906 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 940
Cdd:cd00116 281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 3.40e-23

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: 95.82  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196   468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 75709196   544 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 585
Cdd:pfam17776  81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-530 1.54e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.12  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 153 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 229
Cdd:COG5635 168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 230 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 308
Cdd:COG5635 240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 309 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 387
Cdd:COG5635 305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 388 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 452
Cdd:COG5635 376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 453 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 529
Cdd:COG5635 456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                .
gi 75709196 530 R 530
Cdd:COG5635 522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 762-970 2.82e-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: 91.78  E-value: 2.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 762 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 841
Cdd:COG5238 209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 842 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 920
Cdd:COG5238 288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75709196 921 ILCQALENpNCNLKHLRL-KTYETNLEIKKLLEEVKEKN-PKLTIDCNASGA 970
Cdd:COG5238 367 ALAKYLEG-NTTLRELNLgKNNIGKQGAEALIDALQTNRlHTLILDGNLIGA 417
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 8.47e-18

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: 78.78  E-value: 8.47e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75709196    10 LQTLLEQLNEDELKSFKSLLWAFPLEDvLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCK 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEG-LRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 754-962 1.04e-17

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 85.10  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 754 DLLRNHKCnLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSAN-------VLLDEGAMLLYKTMtrpkhfLQMLSLE 826
Cdd:cd00116  17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetgriprGLQSLLQGLTKGCG------LQELDLS 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 827 NCRLTEASCKDLAAVLvVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSLT 906
Cdd:cd00116  90 DNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLK 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75709196 907 NLDLSINQI-ARGLWILCQALENpNCNLKHLRLKTYETNLEIKKLLEEVKEKNPKLT 962
Cdd:cd00116 169 ELNLANNGIgDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 412-466 2.75e-12

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: 62.20  E-value: 2.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 75709196   412 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 466
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 671-887 3.20e-11

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: 65.84  E-value: 3.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 671 FSSNSNLKFLEVKQSFLSDSSVRILCDHVTRSTCHLQK-VEIKNVTPDTAYRDFCLAFIGKKTLTHLTLA-GHIEWERTM 748
Cdd:cd00116 104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKlVLGRNRLEGASCEALAKALRANRDLKELNLAnNGIGDAGIR 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 749 MLmlCDLLRnHKCNLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHFLQMLSLENC 828
Cdd:cd00116 184 AL--AEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75709196 829 RLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSI 887
Cdd:cd00116 261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-83 9.06e-10

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: 55.99  E-value: 9.06e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75709196  10 LQTLLEQLNEDELKSFKSLLWAFPLEDVlQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTEL 83
Cdd:cd08321   4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 793-938 3.47e-09

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: 60.19  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 793 HLRLSANVLLDEGAMLLYKTMTrpKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSY 872
Cdd:COG5238 157 HLLGLAARLGLLAAISMAKALQ--NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75709196 873 pDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLWILCQALENpNCNLKHLRL 938
Cdd:COG5238 235 -NKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIgAEGAIALAKALQG-NTTLTSLDL 299
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
660-915 1.38e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 660 SLRLWTDFCSLFSSNSNLKFLEVKQSFLSDSSVRILCDHVTRSTCHLQKVEIKNVTPDTAYRDFCLAFIGKKTLTHLTLA 739
Cdd:COG4886  13 LLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDL 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 740 GHIEWERTMMLMLCDLLRNHKcNLQYLRLGGHCATpeqwaEFFYVLKANQSLKHLRLSANVLLDEGAMLlyKTMTRpkhf 819
Cdd:COG4886  93 GDLTNLTELDLSGNEELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTDLPEPL--GNLTN---- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 820 LQMLSLENCRLTeasckDLAAVLVVSKKLTHLCLAKNPIGDTGVKFlcEGLSypdcKLQTLVLQQCSITKLgcrylSEAL 899
Cdd:COG4886 161 LKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLPEPL--GNLT----NLEELDLSGNQLTDL-----PEPL 224

                       250
                ....*....|....*.
gi 75709196 900 QEACSLTNLDLSINQI 915
Cdd:COG4886 225 ANLTNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
785-938 4.37e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196 785 LKANQSLKHLRLSANVLLDegamlLYKTMTRPKHfLQMLSLENCRLTeasckDLAAVLVVSKKLTHLCLAKNPIgdTGVK 864
Cdd:COG4886 109 LSNLTNLESLDLSGNQLTD-----LPEELANLTN-LKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQL--TDLP 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75709196 865 FLCEGLSypdcKLQTLVLQQCSITKLgcrylSEALQEACSLTNLDLSINQIARglwiLCQALENPNcNLKHLRL 938
Cdd:COG4886 176 EELGNLT----NLKELDLSNNQITDL-----PEPLGNLTNLEELDLSGNQLTD----LPEPLANLT-NLETLDL 235
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 1.97e-03

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: 37.67  E-value: 1.97e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75709196  10 LQTLLEQLNEDELKSFKSLlwafpLEDVLQKTPwSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAK 88
Cdd:cd08305   1 LLTGLENITDEEFKMFKSL-----LASELKLTR-KMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 173-311 6.22e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75709196    173 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 247
Cdd:smart00382   4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75709196    248 --ILFvvdgLDElkvpPGALIQDICGDWEKKKPVPVLLGSLLKRKmlPRAALLVTTRPRALRDLQL 311
Cdd:smart00382  79 pdVLI----LDE----ITSLLDAEQEALLLLLEELRLLLLLKSEK--NLTVILTTNDEKDLGPALL 134
 
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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