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Conserved domains on  [gi|33667040|ref|NP_789781|]
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NACHT, LRR and PYD domains-containing protein 8 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 781-1007 3.22e-36

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: 139.80  E-value: 3.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  781 RVLRSPRCrLQCLRLEDCLATPRIWTDLGNNLQGNGHLKTLILRKNSLEN-------CGAYYLSVAQLERLSIENCNLTQ 853
Cdd:cd00116   17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiprglqsLLQGLTKGCGLQELDLSDNALGP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  854 LTCESLASCLrQSKMLTHLSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSF 933
Cdd:cd00116   96 DGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLAN 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667040  934 NSLKDDGVILLCEALKNpDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSS 1007
Cdd:cd00116  175 NGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLS 247
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 41-123 6.36e-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: 110.79  E-value: 6.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040   41 VMLYMRNVSHEELQRFKQLLLTE-LSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMCVVVRR 119
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEEsLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 33667040  120 EINA 123
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 509-624 2.01e-25

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: 101.98  E-value: 2.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    509 TFQEFFAALFYVLCFPQRLKN-----FHVLSHVNIQRLIASPRGSK-SYLSHMGLFLFGFLNEACASAVEQSFQCKVSFG 582
Cdd:pfam17776    3 SFQEFFAALFYVLSFKEEKSNplkefFGLRKRESLKSLLDKALKSKnGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 33667040    583 NKRKLLKVIPLLHKCDPPSPGSgvPQLFYCLHEIREEAFVSQ 624
Cdd:pfam17776   83 IKQELLQWIKSLIQKELSSERF--LNLFHCLYELQDESFVKE 122
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 205-372 2.40e-23

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member pfam05729:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 166  Bit Score: 97.76  E-value: 2.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    205 TVAIQGAPGIGKTILAKKVMFEWARNKFYAHKRWcAFYFHCQEVNQTTDQ-SFSELIEQKWPGSQDLVSK----IMSKPD 279
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDF-VFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    280 QLLLLLDGFEELTStlidrleDLSEDwRQKLPGSVLLSSLLSKTMLPEATLLIMIRFTSWQTCKPLLKCPSLVTLPGFNT 359
Cdd:pfam05729   81 RLLLILDGLDELVS-------DLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|...
gi 33667040    360 MEKIKYFQMYFGH 372
Cdd:pfam05729  153 SDRKQYVRKYFSD 165
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 449-505 5.34e-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: 61.43  E-value: 5.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 33667040    449 AQLEGLCHLAADSMWHRKWVLGKEDLEEAKLDQTGVTAFLGMSILRRIAGEEDHYVF 505
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 693-798 1.45e-05

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: 48.12  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  693 QDLCSVFATNDKLEVLTMTNSVLGPPFLKALAAALRHPQCKLQKLLLRRVNSTMLN-QDLIGVLTGNQHLRYLEIQHVEV 771
Cdd:cd00116  211 SALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGaKDLAEVLAEKESLLELDLRGNKF 290

                         90       100
                 ....*....|....*....|....*..
gi 33667040  772 ESKAVKLLCRVLRSPRCRLQCLRLEDC 798
Cdd:cd00116  291 GEEGAQLLAESLLEPGNELESLWVKDD 317
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 781-1007 3.22e-36

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: 139.80  E-value: 3.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  781 RVLRSPRCrLQCLRLEDCLATPRIWTDLGNNLQGNGHLKTLILRKNSLEN-------CGAYYLSVAQLERLSIENCNLTQ 853
Cdd:cd00116   17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiprglqsLLQGLTKGCGLQELDLSDNALGP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  854 LTCESLASCLrQSKMLTHLSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSF 933
Cdd:cd00116   96 DGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLAN 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667040  934 NSLKDDGVILLCEALKNpDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSS 1007
Cdd:cd00116  175 NGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLS 247
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 41-123 6.36e-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: 110.79  E-value: 6.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040   41 VMLYMRNVSHEELQRFKQLLLTE-LSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMCVVVRR 119
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEEsLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 33667040  120 EINA 123
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 509-624 2.01e-25

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: 101.98  E-value: 2.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    509 TFQEFFAALFYVLCFPQRLKN-----FHVLSHVNIQRLIASPRGSK-SYLSHMGLFLFGFLNEACASAVEQSFQCKVSFG 582
Cdd:pfam17776    3 SFQEFFAALFYVLSFKEEKSNplkefFGLRKRESLKSLLDKALKSKnGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 33667040    583 NKRKLLKVIPLLHKCDPPSPGSgvPQLFYCLHEIREEAFVSQ 624
Cdd:pfam17776   83 IKQELLQWIKSLIQKELSSERF--LNLFHCLYELQDESFVKE 122
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 205-372 2.40e-23

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: 97.76  E-value: 2.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    205 TVAIQGAPGIGKTILAKKVMFEWARNKFYAHKRWcAFYFHCQEVNQTTDQ-SFSELIEQKWPGSQDLVSK----IMSKPD 279
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDF-VFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    280 QLLLLLDGFEELTStlidrleDLSEDwRQKLPGSVLLSSLLSKTMLPEATLLIMIRFTSWQTCKPLLKCPSLVTLPGFNT 359
Cdd:pfam05729   81 RLLLILDGLDELVS-------DLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|...
gi 33667040    360 MEKIKYFQMYFGH 372
Cdd:pfam05729  153 SDRKQYVRKYFSD 165
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 708-1004 2.68e-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: 2.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  708 LTMTNSVLG--PPFLKALAAALRHPQCKLQKLLLRRVNSTMLNQDLIGvlTGNQHLRYLEIQHVEVESKAVKLLCRVLRS 785
Cdd:COG5238  105 LAETATAVAtpPPDLRRIMAKTLEDSLILYLALPRRINLIQVLKDPLG--GNAVHLLGLAARLGLLAAISMAKALQNNSV 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  786 PRCRLQCLRLEDCLATpriwtDLGNNLQGNGHLKTLILRKNSLENCGAyylsvaqlerlsiencnltqltcESLASCLRQ 865
Cdd:COG5238  183 ETVYLGCNQIGDEGIE-----ELAEALTQNTTVTTLWLKRNPIGDEGA-----------------------EILAEALKG 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  866 SKMLTHLSLAENALKDEGAKHIWNALPHLRcPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVILLC 945
Cdd:COG5238  235 NKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALA 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 33667040  946 EALKNpDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEA 1004
Cdd:COG5238  314 EGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKY 371
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 40-114 2.40e-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: 77.24  E-value: 2.40e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667040     40 GVMLYMRNVSHEELQRFKQLLLTELSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMC 114
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
204-520 2.96e-14

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.54  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  204 KTVAIQGAPGIGKTILAKKVMFEWARNKFYAHkRWCAFYFHCQEVNqtTDQSFSELIEQKW----PGSQDLVSKIMSKpD 279
Cdd:COG5635  181 KRLLILGEPGSGKTTLLRYLALELAERYLDAE-DPIPILIELRDLA--EEASLEDLLAEALekrgGEPEDALERLLRN-G 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  280 QLLLLLDGFEELTST-----LIDRLEDLSEDWrqklpgsvllssllsktmlPEATLLIMIRFTSWQTcKPLLKCPSLVTL 354
Cdd:COG5635  257 RLLLLLDGLDEVPDEadrdeVLNQLRRFLERY-------------------PKARVIITSRPEGYDS-SELEGFEVLELA 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  355 PgFNTMEKIKYFQMYFGHTEE-GDQVLSFAMENTILFSMCRVPVVCWMVCSglkqQMERGNNLTQscpNATSVFVRYISS 433
Cdd:COG5635  317 P-LSDEQIEEFLKKWFEATERkAERLLEALEENPELRELARNPLLLTLLAL----LLRERGELPD---TRAELYEQFVEL 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  434 LF----PTRAENFSRKIHQAQLEG-LCHLAAdSMWHRkwvlGKEDLEEAKLDQTgVTAFLGMS-----ILRRIAGE---- 499
Cdd:COG5635  389 LLerwdEQRGLTIYRELSREELRElLSELAL-AMQEN----GRTEFAREELEEI-LREYLGRRkdaeaLLDELLLRtgll 462

                        330       340
                 ....*....|....*....|....*
gi 33667040  500 ----EDHYVFTLVTFQEFFAALFYV 520
Cdd:COG5635  463 vergEGRYSFAHRSFQEYLAARALV 487
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 449-505 5.34e-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: 61.43  E-value: 5.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 33667040    449 AQLEGLCHLAADSMWHRKWVLGKEDLEEAKLDQTGVTAFLGMSILRRIAGEEDHYVF 505
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 693-798 1.45e-05

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: 48.12  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  693 QDLCSVFATNDKLEVLTMTNSVLGPPFLKALAAALRHPQCKLQKLLLRRVNSTMLN-QDLIGVLTGNQHLRYLEIQHVEV 771
Cdd:cd00116  211 SALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGaKDLAEVLAEKESLLELDLRGNKF 290

                         90       100
                 ....*....|....*....|....*..
gi 33667040  772 ESKAVKLLCRVLRSPRCRLQCLRLEDC 798
Cdd:cd00116  291 GEEGAQLLAESLLEPGNELESLWVKDD 317
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
923-949 8.83e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.39  E-value: 8.83e-04
                            10        20
                    ....*....|....*....|....*..
gi 33667040     923 NKTLKSLDLSFNSLKDDGVILLCEALK 949
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
922-945 2.92e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 36.06  E-value: 2.92e-03
                           10        20
                   ....*....|....*....|....
gi 33667040    922 KNKTLKSLDLSFNSLKDDGVILLC 945
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 781-1007 3.22e-36

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: 139.80  E-value: 3.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  781 RVLRSPRCrLQCLRLEDCLATPRIWTDLGNNLQGNGHLKTLILRKNSLEN-------CGAYYLSVAQLERLSIENCNLTQ 853
Cdd:cd00116   17 ELLPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiprglqsLLQGLTKGCGLQELDLSDNALGP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  854 LTCESLASCLrQSKMLTHLSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSF 933
Cdd:cd00116   96 DGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLAN 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667040  934 NSLKDDGVILLCEALKNpDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSS 1007
Cdd:cd00116  175 NGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLS 247
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 717-965 1.78e-31

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: 125.93  E-value: 1.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  717 PPFLKALAAALRHpQCKLQKLLLRRVNSTMLNQDLIGVLTGNQHLRYLEIQHVEVESKAVKLLCRVLRSPRCRLQCLRLE 796
Cdd:cd00116   67 PRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  797 DCLATPRIWTDLGNNLQGNGHLKTLILRKNSLENCGAYYLSVA-----QLERLSIENCNLTQLTCESLASCLRQSKMLTH 871
Cdd:cd00116  146 RNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGlkancNLEVLDLNNNGLTDEGASALAETLASLKSLEV 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  872 LSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVILLCEALKNP 951
Cdd:cd00116  226 LNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEP 305

                        250
                 ....*....|....
gi 33667040  952 DCTLQILELENCLF 965
Cdd:cd00116  306 GNELESLWVKDDSF 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 41-123 6.36e-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: 110.79  E-value: 6.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040   41 VMLYMRNVSHEELQRFKQLLLTE-LSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMCVVVRR 119
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEEsLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 33667040  120 EINA 123
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 509-624 2.01e-25

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: 101.98  E-value: 2.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    509 TFQEFFAALFYVLCFPQRLKN-----FHVLSHVNIQRLIASPRGSK-SYLSHMGLFLFGFLNEACASAVEQSFQCKVSFG 582
Cdd:pfam17776    3 SFQEFFAALFYVLSFKEEKSNplkefFGLRKRESLKSLLDKALKSKnGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 33667040    583 NKRKLLKVIPLLHKCDPPSPGSgvPQLFYCLHEIREEAFVSQ 624
Cdd:pfam17776   83 IKQELLQWIKSLIQKELSSERF--LNLFHCLYELQDESFVKE 122
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 205-372 2.40e-23

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: 97.76  E-value: 2.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    205 TVAIQGAPGIGKTILAKKVMFEWARNKFYAHKRWcAFYFHCQEVNQTTDQ-SFSELIEQKWPGSQDLVSK----IMSKPD 279
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDF-VFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040    280 QLLLLLDGFEELTStlidrleDLSEDwRQKLPGSVLLSSLLSKTMLPEATLLIMIRFTSWQTCKPLLKCPSLVTLPGFNT 359
Cdd:pfam05729   81 RLLLILDGLDELVS-------DLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|...
gi 33667040    360 MEKIKYFQMYFGH 372
Cdd:pfam05729  153 SDRKQYVRKYFSD 165
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 819-1010 8.90e-21

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: 94.34  E-value: 8.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  819 KTLILRKNSLENCGAYYL--SVAQLERLSIENCNLTQLTCESLASCLRQSKMLTHLSLAENALkdEGAKHIWNALPH-LR 895
Cdd:cd00116    1 LQLSLKGELLKTERATELlpKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNET--GRIPRGLQSLLQgLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  896 --CPLQRLVLRKCDLTFNCCQdMISALCKNKTLKSLDLSFNSLKDDGVILLCEALKNPDCTLQILELENCLFTSICCQAM 973
Cdd:cd00116   79 kgCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667040  974 ASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSSQKK 1010
Cdd:cd00116  158 AKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN 194
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 708-1004 2.68e-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: 2.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  708 LTMTNSVLG--PPFLKALAAALRHPQCKLQKLLLRRVNSTMLNQDLIGvlTGNQHLRYLEIQHVEVESKAVKLLCRVLRS 785
Cdd:COG5238  105 LAETATAVAtpPPDLRRIMAKTLEDSLILYLALPRRINLIQVLKDPLG--GNAVHLLGLAARLGLLAAISMAKALQNNSV 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  786 PRCRLQCLRLEDCLATpriwtDLGNNLQGNGHLKTLILRKNSLENCGAyylsvaqlerlsiencnltqltcESLASCLRQ 865
Cdd:COG5238  183 ETVYLGCNQIGDEGIE-----ELAEALTQNTTVTTLWLKRNPIGDEGA-----------------------EILAEALKG 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  866 SKMLTHLSLAENALKDEGAKHIWNALPHLRcPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVILLC 945
Cdd:COG5238  235 NKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALA 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 33667040  946 EALKNpDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEA 1004
Cdd:COG5238  314 EGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKY 371
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 40-114 2.40e-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: 77.24  E-value: 2.40e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667040     40 GVMLYMRNVSHEELQRFKQLLLTELSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMC 114
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
204-520 2.96e-14

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.54  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  204 KTVAIQGAPGIGKTILAKKVMFEWARNKFYAHkRWCAFYFHCQEVNqtTDQSFSELIEQKW----PGSQDLVSKIMSKpD 279
Cdd:COG5635  181 KRLLILGEPGSGKTTLLRYLALELAERYLDAE-DPIPILIELRDLA--EEASLEDLLAEALekrgGEPEDALERLLRN-G 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  280 QLLLLLDGFEELTST-----LIDRLEDLSEDWrqklpgsvllssllsktmlPEATLLIMIRFTSWQTcKPLLKCPSLVTL 354
Cdd:COG5635  257 RLLLLLDGLDEVPDEadrdeVLNQLRRFLERY-------------------PKARVIITSRPEGYDS-SELEGFEVLELA 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  355 PgFNTMEKIKYFQMYFGHTEE-GDQVLSFAMENTILFSMCRVPVVCWMVCSglkqQMERGNNLTQscpNATSVFVRYISS 433
Cdd:COG5635  317 P-LSDEQIEEFLKKWFEATERkAERLLEALEENPELRELARNPLLLTLLAL----LLRERGELPD---TRAELYEQFVEL 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  434 LF----PTRAENFSRKIHQAQLEG-LCHLAAdSMWHRkwvlGKEDLEEAKLDQTgVTAFLGMS-----ILRRIAGE---- 499
Cdd:COG5635  389 LLerwdEQRGLTIYRELSREELRElLSELAL-AMQEN----GRTEFAREELEEI-LREYLGRRkdaeaLLDELLLRtgll 462

                        330       340
                 ....*....|....*....|....*
gi 33667040  500 ----EDHYVFTLVTFQEFFAALFYV 520
Cdd:COG5635  463 vergEGRYSFAHRSFQEYLAARALV 487
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 449-505 5.34e-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: 61.43  E-value: 5.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 33667040    449 AQLEGLCHLAADSMWHRKWVLGKEDLEEAKLDQTGVTAFLGMSILRRIAGEEDHYVF 505
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
807-993 8.22e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 8.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  807 DLGNN--LQGNGHLKTLILRKNSLENCGAYYLSVAQLERLSIENCNLTQLTcESLASClrqsKMLTHLSLAENALKDega 884
Cdd:COG4886  102 DLSGNeeLSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLP-EPLGNL----TNLKSLDLSNNQLTD--- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  885 khiwnalphLRCPLQRLV-LRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDdgvilLCEALKNpdCT-LQILELEN 962
Cdd:COG4886  174 ---------LPEELGNLTnLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTD-----LPEPLAN--LTnLETLDLSN 237

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667040  963 CLFTSIccqamaSMLRKNQHLRHLDLSKNAI 993
Cdd:COG4886  238 NQLTDL------PELGNLTNLEELDLSNNQL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
806-993 2.87e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.88  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  806 TDLGNNLQGNGHLKTLILRKNSLENCGAYYLSVAQLERLSIENCNLTQLTcESLASClrqsKMLTHLSLAENALKDegak 885
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLP-EELGNL----TNLKELDLSNNQITD---- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  886 hiwnaLPHlrcPLQRLV-LRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVIllcEALKNpdctLQILELENCL 964
Cdd:COG4886  197 -----LPE---PLGNLTnLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPEL---GNLTN----LEELDLSNNQ 261

                        170       180
                 ....*....|....*....|....*....
gi 33667040  965 FTSIccqamaSMLRKNQHLRHLDLSKNAI 993
Cdd:COG4886  262 LTDL------PPLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
806-962 4.51e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  806 TDLGNNLQGNGHLKTLILRKNSLENcgayyLSVA-----QLERLSIENCNLTQLTcESLASClrqsKMLTHLSLAENALK 880
Cdd:COG4886  172 TDLPEELGNLTNLKELDLSNNQITD-----LPEPlgnltNLEELDLSGNQLTDLP-EPLANL----TNLETLDLSNNQLT 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  881 DegakhiwnaLPHL-RCP-LQRLVLRKCDLTFnccqdmISALCKNKTLKSLDLSFNSLKDDGVILLCEALKNPDCTLQIL 958
Cdd:COG4886  242 D---------LPELgNLTnLEELDLSNNQLTD------LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306


                 ....
gi 33667040  959 ELEN 962
Cdd:COG4886  307 LLNL 310
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 922-1009 8.42e-07

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: 52.87  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  922 KNKTLKSLDLSFNSLKDDGVILLCEALKNPDcTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTL 1001
Cdd:COG5238  178 QNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL 256


                 ....*...
gi 33667040 1002 CEAFSSQK 1009
Cdd:COG5238  257 AEALKNNT 264
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
804-993 7.41e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.55  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  804 IWTDLGNNLQGNGHLKTLILRKNSLENCGAYYLSVAQLERLSIENCNLTQLTCESLASClrqsKMLTHLSLAENalkdeg 883
Cdd:COG4886   37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDL----TNLTELDLSGN------ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  884 akhiwNALPHLRcPLQRLVLRKCDLTfnccqDMISALCKNKTLKSLDLSFNSLKDdgvilLCEALKNpdCT-LQILELEN 962
Cdd:COG4886  107 -----EELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTD-----LPEPLGN--LTnLKSLDLSN 168

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667040  963 CLFTSIccqamASMLRKNQHLRHLDLSKNAI 993
Cdd:COG4886  169 NQLTDL-----PEELGNLTNLKELDLSNNQI 194
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 693-798 1.45e-05

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: 48.12  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  693 QDLCSVFATNDKLEVLTMTNSVLGPPFLKALAAALRHPQCKLQKLLLRRVNSTMLN-QDLIGVLTGNQHLRYLEIQHVEV 771
Cdd:cd00116  211 SALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGaKDLAEVLAEKESLLELDLRGNKF 290

                         90       100
                 ....*....|....*....|....*..
gi 33667040  772 ESKAVKLLCRVLRSPRCRLQCLRLEDC 798
Cdd:cd00116  291 GEEGAQLLAESLLEPGNELESLWVKDD 317
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 44-114 2.73e-05

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: 43.06  E-value: 2.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33667040   44 YMRNVSHEELQRFKQLLLTELStgtmpITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMC 114
Cdd:cd08305    4 GLENITDEEFKMFKSLLASELK-----LTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLA 69
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
923-949 8.83e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.39  E-value: 8.83e-04
                            10        20
                    ....*....|....*....|....*..
gi 33667040     923 NKTLKSLDLSFNSLKDDGVILLCEALK 949
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
922-945 2.92e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 36.06  E-value: 2.92e-03
                           10        20
                   ....*....|....*....|....
gi 33667040    922 KNKTLKSLDLSFNSLKDDGVILLC 945
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 817-993 9.39e-03

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.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 39.00  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  817 HLKTLILRKN---SLENCGayylSVAQLERLSIENCNLTQLtcESLASClrqsKMLTHLSLAENALKD----EGAKHiwn 889
Cdd:cd21340   25 NLKVLYLYDNkitKIENLE----FLTNLTHLYLQNNQIEKI--ENLENL----VNLKKLYLGGNRISVveglENLTN--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667040  890 aLPHLRCPLQRLVLRKCdLTFNCcqDMISALCKnkTLKSLDLSFNSLKDDGVIllcEALKNpdctLQILELENCLFTSIc 969
Cdd:cd21340   92 -LEELHIENQRLPPGEK-LTFDP--RSLAALSN--SLRVLNISGNNIDSLEPL---APLRN----LEQLDASNNQISDL- 157

                        170       180
                 ....*....|....*....|....
gi 33667040  970 cQAMASMLRKNQHLRHLDLSKNAI 993
Cdd:cd21340  158 -EELLDLLSSWPSLRELDLTGNPV 180
 
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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