NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46049100|ref|NP_631915|]
View 

NACHT, LRR and PYD domains-containing protein 7 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.05e-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: 164.79  E-value: 1.05e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 46049100    327 EDRRAYFLRHFGDE 340
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 702-969 6.82e-30

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: 121.31  E-value: 6.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  702 KKTLTHLTLAG--HIEWERTMMLMLCDLLRNhkCNLQYLRLGGHCATPEQwAEFFYVLKANQSLKHLRLSANVLLDEGAM 779
Cdd:cd00116   50 QPSLKELCLSLneTGRIPRGLQSLLQGLTKG--CGLQELDLSDNALGPDG-CGVLESLLRSSSLQELKLNNNGLGDRGLR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  780 LLYKTMTRPKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSI 859
Cdd:cd00116  127 LLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  860 TKLGCRYLSEALQEACSLTNLDLSINQIA-RGLWILCQALENPNCNLKHLRLWSCSLMPFYCQHLGSALLSNQKLETLDL 938
Cdd:cd00116  206 TDEGASALAETLASLKSLEVLNLGDNNLTdAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                        250       260       270
                 ....*....|....*....|....*....|.
gi 46049100  939 GQNHLWKSGIIKLFGVLRQRTGSLKILRLKT 969
Cdd:cd00116  286 RGNKFGEEGAQLLAESLLEPGNELESLWVKD 316
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 8.02e-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: 8.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100   10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 46049100   90 EMME 93
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 5.12e-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: 95.05  E-value: 5.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 46049100    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 3.15e-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: 3.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 46049100    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 1.05e-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: 164.79  E-value: 1.05e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 46049100    327 EDRRAYFLRHFGDE 340
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 702-969 6.82e-30

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: 121.31  E-value: 6.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  702 KKTLTHLTLAG--HIEWERTMMLMLCDLLRNhkCNLQYLRLGGHCATPEQwAEFFYVLKANQSLKHLRLSANVLLDEGAM 779
Cdd:cd00116   50 QPSLKELCLSLneTGRIPRGLQSLLQGLTKG--CGLQELDLSDNALGPDG-CGVLESLLRSSSLQELKLNNNGLGDRGLR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  780 LLYKTMTRPKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSI 859
Cdd:cd00116  127 LLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  860 TKLGCRYLSEALQEACSLTNLDLSINQIA-RGLWILCQALENPNCNLKHLRLWSCSLMPFYCQHLGSALLSNQKLETLDL 938
Cdd:cd00116  206 TDEGASALAETLASLKSLEVLNLGDNNLTdAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                        250       260       270
                 ....*....|....*....|....*....|.
gi 46049100  939 GQNHLWKSGIIKLFGVLRQRTGSLKILRLKT 969
Cdd:cd00116  286 RGNKFGEEGAQLLAESLLEPGNELESLWVKD 316
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 8.02e-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: 8.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100   10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 46049100   90 EMME 93
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 5.12e-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: 95.05  E-value: 5.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 46049100    544 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 585
Cdd:pfam17776   81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-530 1.31e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  153 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 229
Cdd:COG5635  168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  230 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 308
Cdd:COG5635  240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  309 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 387
Cdd:COG5635  305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  388 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 452
Cdd:COG5635  376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  453 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 529
Cdd:COG5635  456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                 .
gi 46049100  530 R 530
Cdd:COG5635  522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 734-982 7.17e-21

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: 96.78  E-value: 7.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  734 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 813
Cdd:COG5238  209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  814 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 892
Cdd:COG5238  288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  893 ILCQALENpncnlkhlrlwscslmpfycqhlgsallsNQKLETLDLGQNHLWKSGIIKLFGVLrqRTGSLKILRLKTYET 972
Cdd:COG5238  367 ALAKYLEG-----------------------------NTTLRELNLGKNNIGKQGAEALIDAL--QTNRLHTLILDGNLI 415

                        250
                 ....*....|
gi 46049100  973 NLEIKKLLEE 982
Cdd:COG5238  416 GAEAQQRLEQ 425
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 1.03e-17

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: 78.40  E-value: 1.03e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46049100     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 3.15e-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: 3.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 46049100    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 7.91e-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: 7.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100     173 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 247
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46049100     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 1.05e-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: 164.79  E-value: 1.05e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    172 YTVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSRMGP-CSFAELISKDWPELQDDIP----SILAQAQ 246
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSevwaVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    247 RILFVVDGLDELKVPPGALIQDIcgdwekkkPVPVLLGSLLKRKMLPRAALLVTTRPRALRDLQLLAQQPIYVRVEGFLE 326
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 46049100    327 EDRRAYFLRHFGDE 340
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 702-969 6.82e-30

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: 121.31  E-value: 6.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  702 KKTLTHLTLAG--HIEWERTMMLMLCDLLRNhkCNLQYLRLGGHCATPEQwAEFFYVLKANQSLKHLRLSANVLLDEGAM 779
Cdd:cd00116   50 QPSLKELCLSLneTGRIPRGLQSLLQGLTKG--CGLQELDLSDNALGPDG-CGVLESLLRSSSLQELKLNNNGLGDRGLR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  780 LLYKTMTRPKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSI 859
Cdd:cd00116  127 LLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  860 TKLGCRYLSEALQEACSLTNLDLSINQIA-RGLWILCQALENPNCNLKHLRLWSCSLMPFYCQHLGSALLSNQKLETLDL 938
Cdd:cd00116  206 TDEGASALAETLASLKSLEVLNLGDNNLTdAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                        250       260       270
                 ....*....|....*....|....*....|.
gi 46049100  939 GQNHLWKSGIIKLFGVLRQRTGSLKILRLKT 969
Cdd:cd00116  286 RGNKFGEEGAQLLAESLLEPGNELESLWVKD 316
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 726-986 6.67e-29

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: 118.23  E-value: 6.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  726 DLLRNHKCnLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSAN-------VLLDEGAMLLYKTMtrpkhfLQMLSLE 798
Cdd:cd00116   17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetgriprGLQSLLQGLTKGCG------LQELDLS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  799 NCRLTEASCKDLAAVLVvSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSLT 878
Cdd:cd00116   90 DNALGPDGCGVLESLLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  879 NLDLSINQI-ARGLWILCQALENpNCNLKHLRLWSCSLMPFYCQHLGSALLSNQKLETLDLGQNHLWKSGIIKLFGVLRQ 957
Cdd:cd00116  169 ELNLANNGIgDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLS 247

                        250       260       270
                 ....*....|....*....|....*....|..
gi 46049100  958 RTGSLKILRLktYETNLE---IKKLLEEVKEK 986
Cdd:cd00116  248 PNISLLTLSL--SCNDITddgAKDLAEVLAEK 277
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 8.02e-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: 8.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100   10 LQTLLEQLNEDELKSFKSLLWAFPLEDVLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCKMAKA 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 46049100   90 EMME 93
Cdd:cd08320   81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 723-915 8.89e-28

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: 115.15  E-value: 8.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  723 MLCDLLRNHKCNLQYL-----RLGGHCAtpEQWAEffyVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSL 797
Cdd:cd00116  127 LLAKGLKDLPPALEKLvlgrnRLEGASC--EALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCN-LEVLDL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  798 ENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYPDCKLQTLVLQQCSITKLGCRYLSEALQEACSL 877
Cdd:cd00116  201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 46049100  878 TNLDLSINQI-ARGLWILCQALENPNCNLKHLRLWSCSL 915
Cdd:cd00116  281 LELDLRGNKFgEEGAQLLAESLLEPGNELESLWVKDDSF 319
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 468-585 5.12e-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: 95.05  E-value: 5.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100    468 HLSFQQFLTALFYALEKEEGEDRDGH----AWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEKRAKELEATFGCRMS 543
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 46049100    544 PDIKQELLQCkAHLHANKPLSVTDLKEVLGCLYESQEEELAK 585
Cdd:pfam17776   81 SEIKQELLQW-IKSLIQKELSSERFLNLFHCLYELQDESFVK 121
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-530 1.31e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  153 RNQRFIPFLNPRTPRkltpytVVLHGPAGVGKTTLAKKCMLDWTDCNLSPTLRYAFYLSCKELSrmGPCSFAELISK--- 229
Cdd:COG5635  168 ESLKRLELLEAKKKR------LLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEASLEDLLAEale 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  230 -DWPELQDDIPSILAQaQRILFVVDGLDElkVPPGALIQDICGDwekkkpvpvlLGSLLKRkmLPRAALLVTTRPRALRD 308
Cdd:COG5635  240 kRGGEPEDALERLLRN-GRLLLLLDGLDE--VPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDS 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  309 LQLLAQQpiYVRVEGFLEEDRRAYFLRHFGDEDQAMRAF-ELMRSNAALFQLGSAPAVCWIVCTTLKlqmEKGEDPvptc 387
Cdd:COG5635  305 SELEGFE--VLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP---- 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  388 LTRTGLFLRFLCSRFPQGAQLRG-----------ALRTLSLLAAQGLWAQMSVFHREDLERLGVQ----ESDLRLFLDGD 452
Cdd:COG5635  376 DTRAELYEQFVELLLERWDEQRGltiyrelsreeLRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDEL 455

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  453 ILRQD---RVSKGCYSFIHLSFQQFLTALfyalekeegedrdgHAWDIGDVQKLLSGEERLKNPDLIQVGHFLFGLANEK 529
Cdd:COG5635  456 LLRTGllvERGEGRYSFAHRSFQEYLAAR--------------ALVEELDEELLELLAEHLEDPRWREVLLLLAGLLDDV 521


                 .
gi 46049100  530 R 530
Cdd:COG5635  522 K 522
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 734-982 7.17e-21

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: 96.78  E-value: 7.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  734 NLQYLRLGGHCATPEQWAEFFYVLKANQSLKHLRLSANVLLDEGAMLLYKTMTRPkHFLQMLSLENCRLTEASCKDLAAV 813
Cdd:COG5238  209 TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKA 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  814 LVVSKKLTHLCLAKNPIGDTGVKFLCEGLSYpDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLW 892
Cdd:COG5238  288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIgDEGAI 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  893 ILCQALENpncnlkhlrlwscslmpfycqhlgsallsNQKLETLDLGQNHLWKSGIIKLFGVLrqRTGSLKILRLKTYET 972
Cdd:COG5238  367 ALAKYLEG-----------------------------NTTLRELNLGKNNIGKQGAEALIDAL--QTNRLHTLILDGNLI 415

                        250
                 ....*....|
gi 46049100  973 NLEIKKLLEE 982
Cdd:COG5238  416 GAEAQQRLEQ 425
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 759-999 3.75e-18

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: 88.31  E-value: 3.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  759 ANQSLKHLRLSANVLLDEGAMLLYKTMTRPKHfLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFL 838
Cdd:COG5238  178 QNNSVETVYLGCNQIGDEGIEELAEALTQNTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  839 CEGLSYPDcKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLWILCQALENpNCNLKHLRLWSCSLMP 917
Cdd:COG5238  257 AEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG-NKTLHTLNLAYNGIGA 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  918 FYCQHLGSALLSNQKLETLDLGQNHLWKSGIIKLFGVLRQRTGSLKILRLKTYETNLEIKKLLEEVKEKN-PKLTIDCNA 996
Cdd:COG5238  335 QGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRlHTLILDGNL 414


                 ...
gi 46049100  997 SGA 999
Cdd:COG5238  415 IGA 417
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 1.03e-17

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: 78.40  E-value: 1.03e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46049100     10 LQTLLEQLNEDELKSFKSLLWAFPLEDvLQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTELCK 85
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEPEEG-LRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 765-968 7.24e-13

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: 71.74  E-value: 7.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  765 HLRLSANVLLDEGAMLLYKTMTrpKHFLQMLSLENCRLTEASCKDLAAVLVVSKKLTHLCLAKNPIGDTGVKFLCEGLSY 844
Cdd:COG5238  157 HLLGLAARLGLLAAISMAKALQ--NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  845 pDCKLQTLVLQQCSITKLGCRYLSEALQEACSLTNLDLSINQI-ARGLWILCQALENpNCNLKHLRLWSCSLMPFYCQHL 923
Cdd:COG5238  235 -NKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIgAEGAIALAKALQG-NTTLTSLDLSVNRIGDEGAIAL 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 46049100  924 GSALLSNQKLETLDLGQNHLWKSGIIKLFGVLRQRTgSLKILRLK 968
Cdd:COG5238  313 AEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT-TLHSLDLS 356
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 412-466 3.15e-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: 3.15e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 46049100    412 LRTLSLLAAQGLWAQMSVFHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSF 466
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-83 9.81e-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: 9.81e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46049100   10 LQTLLEQLNEDELKSFKSLLWAFPLEDVlQKTPWSEVEEADGKKLAEILVNTSSENWIRNATVNILEEMNLTEL 83
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
634-993 4.07e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.78  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  634 MDFELDIEFESSNSNLKFLEVKQSFLSDSSVRILCDHVTRSTCHLQKVEIKNVTPDTAYRDFCLAFIGKKTLTHLTLAGH 713
Cdd:COG4886   15 LLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  714 IEWERTMMLMLCDLLRNHKcNLQYLRLGGHCATpeqwaEFFYVLKANQSLKHLRLSANVLLDEGAMLlyKTMTRpkhfLQ 793
Cdd:COG4886   95 LTNLTELDLSGNEELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTDLPEPL--GNLTN----LK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  794 MLSLENCRLTeasckDLAAVLVVSKKLTHLCLAKNPIGDTGVKFlcEGLSypdcKLQTLVLQQCSITKLgcrylSEALQE 873
Cdd:COG4886  163 SLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLPEPL--GNLT----NLEELDLSGNQLTDL-----PEPLAN 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100  874 ACSLTNLDLSINQIARglwilCQALENPNcNLKHLRLWSCSLMPFycqhlgSALLSNQKLETLDLGQNHLWKSGIIKLFG 953
Cdd:COG4886  227 LTNLETLDLSNNQLTD-----LPELGNLT-NLEELDLSNNQLTDL------PPLANLTNLKTLDLSNNQLTDLKLKELEL 294

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 46049100  954 VLRQRTGSLKILRLKTYETNLEIKKLLEEVKEKNPKLTID 993
Cdd:COG4886  295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 2.31e-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: 2.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46049100   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 7.91e-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: 7.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46049100     173 TVVLHGPAGVGKTTLAKKCMLdwtdcNLSPTLRYAFYLSCKELSRMGPCSFAELISKDWPELQDDIPSI---LAQAQR-- 247
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlaLALARKlk 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46049100     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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH