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Conserved domains on  [gi|2462494708|ref|XP_054186921|]
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NACHT, LRR and PYD domains-containing protein 7 isoform X16 [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 ...
 200-368 1.31e-46

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: 164.40  E-value: 1.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  200 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 274
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  275 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 354
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 2462494708  355 EDRRAYFLRHFGDE 368
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 38-121 6.66e-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: 6.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 117
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2462494708  118 EMME 121
Cdd:cd08320     81 EMNE 84
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 779-968 1.20e-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: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  779 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 853
Cdd:cd00116    127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  854 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 933
Cdd:cd00116    201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462494708  934 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 968
Cdd:cd00116    281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 496-613 4.60e-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: 95.44  E-value: 4.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  496 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 571
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462494708  572 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 613
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 ...
 440-494 2.88e-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: 2.88e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462494708  440 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 494
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 ...
 200-368 1.31e-46

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: 164.40  E-value: 1.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  200 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 274
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  275 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 354
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 2462494708  355 EDRRAYFLRHFGDE 368
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 38-121 6.66e-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: 6.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 117
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2462494708  118 EMME 121
Cdd:cd08320     81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 779-968 1.20e-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: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  779 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 853
Cdd:cd00116    127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  854 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 933
Cdd:cd00116    201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462494708  934 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 968
Cdd:cd00116    281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 496-613 4.60e-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: 95.44  E-value: 4.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  496 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 571
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462494708  572 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 613
Cdd:pfam17776   81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
181-558 3.86e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 102.96  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  181 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 257
Cdd:COG5635    168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  258 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 336
Cdd:COG5635    240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  337 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 415
Cdd:COG5635    305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  416 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 480
Cdd:COG5635    376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  481 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 557
Cdd:COG5635    456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                   .
gi 2462494708  558 R 558
Cdd:COG5635    522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 790-998 2.86e-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: 2.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  790 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 869
Cdd:COG5238    209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  870 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 948
Cdd:COG5238    288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462494708  949 ILCQALENpNCNLKHLRL-KTYETNLEIKKLLEEVKEKN-PKLTIDCNASGA 998
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 ...
 38-113 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 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDvLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCK 113
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 ...
 440-494 2.88e-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: 2.88e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462494708  440 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 494
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 201-339 6.99e-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: 38.12  E-value: 6.99e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708   201 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 275
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462494708   276 --ILFvvdgLDElkvpPGALIQDICGDWEKKKPVPVLLGSLLKRKmlPRAALLVTTRPRALRDLQL 339
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 ...
 200-368 1.31e-46

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: 164.40  E-value: 1.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  200 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 274
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  275 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 354
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 2462494708  355 EDRRAYFLRHFGDE 368
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 38-121 6.66e-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: 6.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 117
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2462494708  118 EMME 121
Cdd:cd08320     81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 779-968 1.20e-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: 1.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  779 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 853
Cdd:cd00116    127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  854 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 933
Cdd:cd00116    201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462494708  934 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLKT 968
Cdd:cd00116    281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKD 316
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 496-613 4.60e-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: 95.44  E-value: 4.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  496 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 571
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462494708  572 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 613
Cdd:pfam17776   81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
181-558 3.86e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 102.96  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  181 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 257
Cdd:COG5635    168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  258 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 336
Cdd:COG5635    240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  337 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 415
Cdd:COG5635    305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  416 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 480
Cdd:COG5635    376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  481 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 557
Cdd:COG5635    456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                   .
gi 2462494708  558 R 558
Cdd:COG5635    522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 790-998 2.86e-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: 2.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  790 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 869
Cdd:COG5238    209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  870 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 948
Cdd:COG5238    288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462494708  949 ILCQALENpNCNLKHLRL-KTYETNLEIKKLLEEVKEKN-PKLTIDCNASGA 998
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 ...
 38-113 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 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDvLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCK 113
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEPEEG-LRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 782-990 1.10e-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: 1.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  782 DLLRNHKCnLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSAN-------VLLDEGAMLLYKTMtrpkhfLQMLSLE 854
Cdd:cd00116     17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetgriprGLQSLLQGLTKGCG------LQELDLS 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  855 NCRLTEASCKDLAAVLvVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSLT 934
Cdd:cd00116     90 DNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLK 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462494708  935 NLDLSINQI-ARGLWILCQALENpNCNLKHLRLKTYETNLEIKKLLEEVKEKNPKLT 990
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 ...
 440-494 2.88e-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: 2.88e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462494708  440 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 494
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 699-915 3.38e-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: 3.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  699 FSSNSNLKFLEVKQSFLSDSSVRILCDHVTRSTCHLQK-VEIKNVTPDTAYRDFCLAFIGKKTLTHLTLA-GHIEWERTM 776
Cdd:cd00116    104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKlVLGRNRLEGASCEALAKALRANRDLKELNLAnNGIGDAGIR 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  777 MLmlCDLLRnHKCNLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHFLQMLSLENC 856
Cdd:cd00116    184 AL--AEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462494708  857 RLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSI 915
Cdd:cd00116    261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 38-111 9.52e-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: 9.52e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462494708   38 LQTLLEQLNEDELKSFKSLLWAFPLEDVlQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTEL 111
Cdd:cd08321      4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 821-966 3.69e-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: 3.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  821 HLRLSANVLLDEGAMLLYKTMTrpKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSY 900
Cdd:COG5238    157 HLLGLAARLGLLAAISMAKALQ--NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462494708  901 pDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLWILCQALENpNCNLKHLRL 966
Cdd:COG5238    235 -NKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIgAEGAIALAKALQG-NTTLTSLDL 299
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
688-943 1.31e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  688 SLRLWTDFCSLFSSNSNLKFLEVKQSFLSDSSVRILCDHVTRSTCHLQKVEIKNVTPDTAYRDFCLAFIGKKTLTHLTLA 767
Cdd:COG4886     13 LLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  768 GHIEWERTMMLMLCDLLRNHKcNLQYLRLGGHCATpeqwaEFFYVLKANQSLKHLRLSANVLLDEGAMLlyKTMTRpkhf 847
Cdd:COG4886     93 GDLTNLTELDLSGNEELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTDLPEPL--GNLTN---- 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  848 LQMLSLENCRLTeasckDLAAVLVVSKKLTHLCLAKNPIGDTGVKFlcEGLSypdcKLQTLVLQQCSITKLgcrylSEAL 927
Cdd:COG4886    161 LKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLPEPL--GNLT----NLEELDLSGNQLTDL-----PEPL 224

                          250
                   ....*....|....*.
gi 2462494708  928 QEACSLTNLDLSINQI 943
Cdd:COG4886    225 ANLTNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
813-966 4.48e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708  813 LKANQSLKHLRLSANVLLDegamlLYKTMTRPKHfLQMLSLENCRLTeasckDLAAVLVVSKKLTHLCLAKNPIgdTGVK 892
Cdd:COG4886    109 LSNLTNLESLDLSGNQLTD-----LPEELANLTN-LKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQL--TDLP 175

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462494708  893 FLCEGLSypdcKLQTLVLQQCSITKLgcrylSEALQEACSLTNLDLSINQIARglwiLCQALENPNcNLKHLRL 966
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 ...
 38-116 1.99e-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: 1.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462494708   38 LQTLLEQLNEDELKSFKSLlwafpLEDVLQKTPwSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAK 116
Cdd:cd08305      1 LLTGLENITDEEFKMFKSL-----LASELKLTR-KMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 201-339 6.99e-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: 38.12  E-value: 6.99e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494708   201 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 275
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462494708   276 --ILFvvdgLDElkvpPGALIQDICGDWEKKKPVPVLLGSLLKRKmlPRAALLVTTRPRALRDLQL 339
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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