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Conserved domains on  [gi|755519582|ref|XP_011248866|]
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NACHT, LRR and PYD domains-containing protein 9B isoform X3 [Mus musculus]

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 ...
 692-899 3.69e-33

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: 130.94  E-value: 3.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 692 PHLKYLNLYGTYLSMDVTEKLCA--ALRcSACRVEELLLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLL 769
Cdd:cd00116   51 PSLKELCLSLNETGRIPRGLQSLlqGLT-KGCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 770 CEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTS 849
Cdd:cd00116  129 AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755519582 850 DCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 899
Cdd:cd00116  208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 1.04e-29

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: 115.87  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|...
gi 755519582  299 SVEFYCMSFFDNQ 311
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-86 2.94e-26

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: 103.09  E-value: 2.94e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519582   9 LLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLSIMAQ 86
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQqAWDVALSIFEKMNRTDLCEKAR 79
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 440-555 7.90e-18

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: 80.41  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755519582  512 IYVRQEIICYFKCLGQQECNEklERSQTLFSCLRDSQEERFVRQ 555
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 387-439 2.89e-06

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: 45.25  E-value: 2.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755519582  387 LKTLCTLAVEGMWKELFVFDSEDLRRNGISESDKAVWLKMQFLQTHGNHTVFY 439
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVY 55
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 692-899 3.69e-33

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: 130.94  E-value: 3.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 692 PHLKYLNLYGTYLSMDVTEKLCA--ALRcSACRVEELLLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLL 769
Cdd:cd00116   51 PSLKELCLSLNETGRIPRGLQSLlqGLT-KGCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 770 CEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTS 849
Cdd:cd00116  129 AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755519582 850 DCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 899
Cdd:cd00116  208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 1.04e-29

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: 115.87  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|...
gi 755519582  299 SVEFYCMSFFDNQ 311
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-86 2.94e-26

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: 103.09  E-value: 2.94e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519582   9 LLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLSIMAQ 86
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQqAWDVALSIFEKMNRTDLCEKAR 79
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.82e-18

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 80.33  E-value: 1.82e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755519582    8 GLLKLLQKLSDEEFQRFKELLREEPEkFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLS 82
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGEDaAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 440-555 7.90e-18

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: 80.41  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755519582  512 IYVRQEIICYFKCLGQQECNEklERSQTLFSCLRDSQEERFVRQ 555
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 722-926 9.35e-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: 87.15  E-value: 9.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 722 RVEELLLSYCCLTFIACGHLYEALLsNKHLSLLDLGSNFLEDTGVNLLCEALKDPNcTLKELWLPGCFLTSQCCEEISAV 801
Cdd:COG5238  154 NAVHLLGLAARLGLLAAISMAKALQ-NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEA 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 802 LICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLV 881
Cdd:COG5238  232 LKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAI 310

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755519582 882 VLCEALNHKRcNLKMLGLDKSAFSEESQTLLQDVEKKNNNLNILH 926
Cdd:COG5238  311 ALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 387-439 2.89e-06

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: 45.25  E-value: 2.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755519582  387 LKTLCTLAVEGMWKELFVFDSEDLRRNGISESDKAVWLKMQFLQTHGNHTVFY 439
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVY 55
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
805-832 1.38e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 1.38e-04
                           10        20
                   ....*....|....*....|....*...
gi 755519582   805 NRNLKTLKLGNNNIQDTGVRQLCEALSH 832
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 692-899 3.69e-33

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: 130.94  E-value: 3.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 692 PHLKYLNLYGTYLSMDVTEKLCA--ALRcSACRVEELLLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLL 769
Cdd:cd00116   51 PSLKELCLSLNETGRIPRGLQSLlqGLT-KGCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 770 CEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTS 849
Cdd:cd00116  129 AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755519582 850 DCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 899
Cdd:cd00116  208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 1.04e-29

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: 115.87  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|...
gi 755519582  299 SVEFYCMSFFDNQ 311
Cdd:pfam05729 154 DRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-86 2.94e-26

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: 103.09  E-value: 2.94e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519582   9 LLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLSIMAQ 86
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQqAWDVALSIFEKMNRTDLCEKAR 79
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 668-900 3.34e-26

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: 110.52  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 668 LQSLSCSFMADFGDGSL-------FHTLLQLPHLKYLNLYGTYLSMDVTEKLCAALRCSACRVEELLLSYCCLTFIACGH 740
Cdd:cd00116   77 LTKGCGLQELDLSDNALgpdgcgvLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 741 LYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQD 820
Cdd:cd00116  157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 821 TGVRQLCEALSHPNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGLD 900
Cdd:cd00116  236 AGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.82e-18

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 80.33  E-value: 1.82e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755519582    8 GLLKLLQKLSDEEFQRFKELLREEPEkFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLS 82
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGEDaAVDVTIEILKKINLKDLA 75
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 723-926 3.72e-18

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: 86.64  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 723 VEELLLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLE--DTGVNLLCEALKDpNCTLKELWLPGCFLTSQCCEEISA 800
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 801 VLIcNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGL 880
Cdd:cd00116  104 LLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755519582 881 VVLCEALNHKrCNLKMLGLDKSAFSEESQTLLQDVEKKNNNLNILH 926
Cdd:cd00116  183 RALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 440-555 7.90e-18

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: 80.41  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582  440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755519582  512 IYVRQEIICYFKCLGQQECNEklERSQTLFSCLRDSQEERFVRQ 555
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 722-926 9.35e-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: 87.15  E-value: 9.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 722 RVEELLLSYCCLTFIACGHLYEALLsNKHLSLLDLGSNFLEDTGVNLLCEALKDPNcTLKELWLPGCFLTSQCCEEISAV 801
Cdd:COG5238  154 NAVHLLGLAARLGLLAAISMAKALQ-NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEA 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 802 LICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLV 881
Cdd:COG5238  232 LKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAI 310

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755519582 882 VLCEALNHKRcNLKMLGLDKSAFSEESQTLLQDVEKKNNNLNILH 926
Cdd:COG5238  311 ALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 667-888 6.30e-17

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: 84.46  E-value: 6.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 667 KLQSLSCSFMADFGDGSLFHTLlqlphlkylNLYGTYLSMDVTEKLCAALRCSAcRVEELLLSYCCLTFIACGHLYEALL 746
Cdd:COG5238  164 RLGLLAAISMAKALQNNSVETV---------YLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALK 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 747 SNKHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQL 826
Cdd:COG5238  234 GNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIAL 312

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755519582 827 CEALSHpNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALN 888
Cdd:COG5238  313 AEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 680-847 5.42e-14

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: 73.93  E-value: 5.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 680 GDGSLFHTLLQLPH---LKYLNLYGTYLSMDVTEKLCAALRCSaCRVEELLLSYCCLTFIACGHLYEALLSNKHLSLLDL 756
Cdd:cd00116  150 EGASCEALAKALRAnrdLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 757 GSNFLEDTGVNLLCEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCN 836
Cdd:cd00116  229 GDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNE 308

                        170
                 ....*....|.
gi 755519582 837 LECLGLDLCEF 847
Cdd:cd00116  309 LESLWVKDDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 632-887 1.74e-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: 73.67  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 632 NLYVLDLDSCQFNKRAIQDLCNSMSPTPTVplTAFKLQSLScsfMADFGDGSLFHTLLQLPHLKYLNLYGTYLSMDVTEK 711
Cdd:COG5238  181 SVETVYLGCNQIGDEGIEELAEALTQNTTV--TTLWLKRNP---IGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 712 LCAALRcSACRVEELLLSyccLTFIACGH---LYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGC 788
Cdd:COG5238  256 LAEALK-NNTTVETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYN 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 789 FLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEAL-SHPNcnleCLGLDLC--EFTSDCCKDLALALTTcKTL 865
Cdd:COG5238  331 GIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT----LRELNLGknNIGKQGAEALIDALQT-NRL 405

                        250       260
                 ....*....|....*....|....*
gi 755519582 866 NSLNLDWKTLD---HSGLVVLCEAL 887
Cdd:COG5238  406 HTLILDGNLIGaeaQQRLEQLLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
123-496 1.78e-12

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 71.76  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 123 LIVEVQYKALQEIFDSEsEPVTAIVaGTTGEGKTTFLRKAMLDWASGVLLQNRfQYVFFFSVFSLNNTTELS--LAELIS 200
Cdd:COG5635  163 LLERIESLKRLELLEAK-KKRLLIL-GEPGSGKTTLLRYLALELAERYLDAED-PIPILIELRDLAEEASLEdlLAEALE 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 201 STLPESSETVDDILSDpKRILFILDGFDYLkFDLELRTNLCN---DWRKRLP-TQIVLSS---LLQKIMLPGCslllelg 273
Cdd:COG5635  240 KRGGEPEDALERLLRN-GRLLLLLDGLDEV-PDEADRDEVLNqlrRFLERYPkARVIITSrpeGYDSSELEGF------- 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 274 qisvpkirhllkypRVITMQGFSERSVEFYCMSFFD--NQRGIEVAENLRNN-EVLHLCSNPYLCWMFCSCLkwqfdrEE 350
Cdd:COG5635  311 --------------EVLELAPLSDEQIEEFLKKWFEatERKAERLLEALEENpELRELARNPLLLTLLALLL------RE 370

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 351 EGYFkAKTDAAFFTNFMVSAF-------KSTYAHSPSKQNRARLktLCTLAVEGMWKELFVFDSEDLRRN----GISESD 419
Cdd:COG5635  371 RGEL-PDTRAELYEQFVELLLerwdeqrGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEIlreyLGRRKD 447

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 420 KAVWLKMQFLQTH-----GNHTV-FYHPTLQSYFAAMFYFLKQDKDICvpvigsipQLLGNMYarGQTQWLQLGTFLFGL 493
Cdd:COG5635  448 AEALLDELLLRTGllverGEGRYsFAHRSFQEYLAARALVEELDEELL--------ELLAEHL--EDPRWREVLLLLAGL 517


                 ...
gi 755519582 494 INE 496
Cdd:COG5635  518 LDD 520
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 387-439 2.89e-06

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: 45.25  E-value: 2.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755519582  387 LKTLCTLAVEGMWKELFVFDSEDLRRNGISESDKAVWLKMQFLQTHGNHTVFY 439
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVY 55
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 9-82 7.45e-05

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: 42.13  E-value: 7.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755519582   9 LLKLLQKLSDEEFQRFKELLREEPEKFKlKPISWTKIENSSKESLVTLLNTHY-PGQAWNMMLSLFLQVNREDLS 82
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYgEDYAVEVTVEVLRAINQNDLA 77
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
805-832 1.38e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 1.38e-04
                           10        20
                   ....*....|....*....|....*...
gi 755519582   805 NRNLKTLKLGNNNIQDTGVRQLCEALSH 832
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
683-820 3.04e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 683 SLFHTLLQLPHLKYLNLYGTYLSmDVTEKL--CAALrcsacrvEELLLSYCCLTfiacgHLYEALLSNKHLSLLDLGSNF 760
Cdd:COG4886  127 DLPEELANLTNLKELDLSNNQLT-DLPEPLgnLTNL-------KSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQ 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 761 LEDTGVNLlcEALKdpncTLKELWLPGCFLTSqcceeISAVLICNRNLKTLKLGNNNIQD 820
Cdd:COG4886  194 ITDLPEPL--GNLT----NLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTD 242
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
688-820 1.69e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 688 LLQLPHLKYLNLYGTYLSmDVTEKLcAALRcsacRVEELLLSYCCLTfiacgHLYEALLSNKHLSLLDLGSNFLEDtgvn 767
Cdd:COG4886  109 LSNLTNLESLDLSGNQLT-DLPEEL-ANLT----NLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTD---- 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755519582 768 lLCEALKdpNCT-LKELWLPGCFLTsqcceEISAVLICNRNLKTLKLGNNNIQD 820
Cdd:COG4886  174 -LPEELG--NLTnLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTD 219
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
743-871 4.00e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519582 743 EALLSNKHLSLLDLGSNFLEDTGVNLlcEALKDpnctLKELWLPGCFLTSqcceeISAVLICNRNLKTLKLGNNNIQDtg 822
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEEL--ANLTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-- 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 755519582 823 vrqLCEALShpNC-NLECLGLDLCEFTsdcckDLALALTTCKTLNSLNLD 871
Cdd:COG4886  174 ---LPEELG--NLtNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLS 213
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
748-775 9.32e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 9.32e-03
                           10        20
                   ....*....|....*....|....*...
gi 755519582   748 NKHLSLLDLGSNFLEDTGVNLLCEALKD 775
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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