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Conserved domains on  [gi|568945681|ref|XP_006540002|]
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NACHT, LRR and PYD domains-containing protein 9B isoform X1 [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 ...
 752-955 4.98e-34

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: 133.25  E-value: 4.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  752 HLSLVENPLKNKGVMSLCEMLKDpSCVLQSLMLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKD 831
Cdd:cd00116    57 CLSLNETGRIPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  832 PNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDL 911
Cdd:cd00116   135 LPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASAL 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568945681  912 ALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 955
Cdd:cd00116   214 AETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 9.54e-30

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: 9.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|...
gi 568945681   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 2.64e-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: 2.64e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568945681    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 6.98e-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: 6.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568945681   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 2.72e-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: 2.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568945681   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 ...
 752-955 4.98e-34

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: 133.25  E-value: 4.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  752 HLSLVENPLKNKGVMSLCEMLKDpSCVLQSLMLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKD 831
Cdd:cd00116    57 CLSLNETGRIPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  832 PNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDL 911
Cdd:cd00116   135 LPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASAL 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568945681  912 ALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 955
Cdd:cd00116   214 AETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 9.54e-30

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: 9.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|...
gi 568945681   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 2.64e-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: 2.64e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568945681    9 LLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLSIMAQ 86
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQqAWDVALSIFEKMNRTDLCEKAR 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 667-943 1.65e-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: 92.55  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  667 KLQSLSCSFMADFGDGSLFHTLlqlphlkylNLYGTYLSMDVTEKLCAALRCSAcRVEELLLGKCGISSKACGIIAISLI 746
Cdd:COG5238   164 RLGLLAAISMAKALQNNSVETV---------YLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  747 -NSKVKHLSLVENPLKNKGVMSLCEMLKDPSCVlQSLMLSyccLTFIACGH---LYEALLSNKHLSLLDLGSNFLEDTGV 822
Cdd:COG5238   234 gNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGA 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  823 NLLCEALKDpNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEAL-SHPNcnleCLGLDLC 901
Cdd:COG5238   310 IALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT----LRELNLG 384

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568945681  902 --EFTSDCCKDLALALTTcKTLNSLNLDWKTLD---HSGLVVLCEAL 943
Cdd:COG5238   385 knNIGKQGAEALIDALQT-NRLHTLILDGNLIGaeaQQRLEQLLERI 430
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.79e-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: 80.71  E-value: 1.79e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945681     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 6.98e-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: 6.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568945681   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 2.72e-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: 2.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568945681   387 LKTLCTLAVEGMWKELFVFDSEDLRRNGISESDKAVWLKMQFLQTHGNHTVFY 439
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVY 55
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
861-888 1.67e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 1.67e-04
                            10        20
                    ....*....|....*....|....*...
gi 568945681    861 NRNLKTLKLGNNNIQDTGVRQLCEALSH 888
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 ...
 752-955 4.98e-34

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: 133.25  E-value: 4.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  752 HLSLVENPLKNKGVMSLCEMLKDpSCVLQSLMLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKD 831
Cdd:cd00116    57 CLSLNETGRIPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  832 PNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDL 911
Cdd:cd00116   135 LPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASAL 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568945681  912 ALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGL 955
Cdd:cd00116   214 AETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 692-956 7.03e-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: 124.00  E-value: 7.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  692 PHLKYLNLYGTYLSMDVTEKLCA--ALRcSACRVEELLLGKCGISSKACGIIAISLINSKVKHLSLVENPLKNKGVMSLC 769
Cdd:cd00116    51 PSLKELCLSLNETGRIPRGLQSLlqGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  770 EMLKDPSCVLQSLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCFLTSQ 849
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  850 CCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWK 929
Cdd:cd00116   209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                         250       260
                  ....*....|....*....|....*..
gi 568945681  930 TLDHSGLVVLCEALNHKRCNLKMLGLD 956
Cdd:cd00116   289 KFGEEGAQLLAESLLEPGNELESLWVK 315
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-311 9.54e-30

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: 9.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   144 TAIVAGTTGEGKTTFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   219 RILFILDGFDYLKFDLELRTNLCndwrkrlPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSER 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|...
gi 568945681   299 SVEFYCMSFFDNQ 311
Cdd:pfam05729  154 DRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 668-903 2.06e-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: 110.91  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  668 LQSLSCSFMADFGDGSL-------FHTLLQLPHLKYLNLYGTYLSMDVTEKLCAALRCSACRVEELLLGKCGISSKACGI 740
Cdd:cd00116    77 LTKGCGLQELDLSDNALgpdgcgvLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  741 IAISLI-NSKVKHLSLVENPLKNKGVMSLCEMLKDpSCVLQSLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLED 819
Cdd:cd00116   157 LAKALRaNRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  820 TGVNLLCEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCNLECLGLD 899
Cdd:cd00116   236 AGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315


                  ....
gi 568945681  900 LCEF 903
Cdd:cd00116   316 DDSF 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-86 2.64e-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: 2.64e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568945681    9 LLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQ-AWNMMLSLFLQVNREDLSIMAQ 86
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQqAWDVALSIFEKMNRTDLCEKAR 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 667-943 1.65e-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: 92.55  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  667 KLQSLSCSFMADFGDGSLFHTLlqlphlkylNLYGTYLSMDVTEKLCAALRCSAcRVEELLLGKCGISSKACGIIAISLI 746
Cdd:COG5238   164 RLGLLAAISMAKALQNNSVETV---------YLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  747 -NSKVKHLSLVENPLKNKGVMSLCEMLKDPSCVlQSLMLSyccLTFIACGH---LYEALLSNKHLSLLDLGSNFLEDTGV 822
Cdd:COG5238   234 gNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGA 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  823 NLLCEALKDpNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEAL-SHPNcnleCLGLDLC 901
Cdd:COG5238   310 IALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT----LRELNLG 384

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568945681  902 --EFTSDCCKDLALALTTcKTLNSLNLDWKTLD---HSGLVVLCEAL 943
Cdd:COG5238   385 knNIGKQGAEALIDALQT-NRLHTLILDGNLIGaeaQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 722-944 1.04e-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: 90.23  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  722 RVEELLLGKCGISSKACGIIAISLINSKVKHLSLVENPLKNKGVMSLCEMLKDPSCVlQSLMLSYCCLTFIACGHLYEAL 801
Cdd:COG5238   154 NAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTV-TTLWLKRNPIGDEGAEILAEAL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  802 LSNKHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQ 881
Cdd:COG5238   233 KGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIA 311

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568945681  882 LCEALSHpNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALN 944
Cdd:COG5238   312 LAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.79e-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: 80.71  E-value: 1.79e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945681     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 6.98e-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: 6.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681   440 HPTLQSYFAAMFYFLKQDKDICVPVI--------GSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQP 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568945681   512 IYVRQEIICYFKCLGQQECNEklERSQTLFSCLRDSQEERFVRQ 555
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 795-982 2.62e-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: 85.61  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  795 GHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKDPNcTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNI 874
Cdd:COG5238   170 AISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  875 QDTGVRQLCEALSHpNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRcNLKMLG 954
Cdd:COG5238   249 GDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLN 326

                         170       180
                  ....*....|....*....|....*...
gi 568945681  955 LDKSAFSEESQTLLQDVEKKNNNLNILH 982
Cdd:COG5238   327 LAYNGIGAQGAIALAKALQENTTLHSLD 354
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
123-591 3.87e-13

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 73.69  E-value: 3.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  123 LIVEVQYKALQEIFDSEsEPVTAIVaGTTGEGKTTFLRKAMLDWASGVLLQNRfQYVFFFSVFSLNNTTELS--LAELIS 200
Cdd:COG5635   163 LLERIESLKRLELLEAK-KKRLLIL-GEPGSGKTTLLRYLALELAERYLDAED-PIPILIELRDLAEEASLEdlLAEALE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  201 STLPESSETVDDILSDpKRILFILDGFDYLkFDLELRTNLCN---DWRKRLP-TQIVLSS---LLQKIMLPGCslllelg 273
Cdd:COG5635   240 KRGGEPEDALERLLRN-GRLLLLLDGLDEV-PDEADRDEVLNqlrRFLERYPkARVIITSrpeGYDSSELEGF------- 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  274 qisvpkirhllkypRVITMQGFSERSVEFYCMSFFD--NQRGIEVAENLRNN-EVLHLCSNPYLCWMFCSCLkwqfdrEE 350
Cdd:COG5635   311 --------------EVLELAPLSDEQIEEFLKKWFEatERKAERLLEALEENpELRELARNPLLLTLLALLL------RE 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  351 EGYFkAKTDAAFFTNFMVSAF-------KSTYAHSPSKQNRARLktLCTLAVEGMWKELFVFDSEDLRRN----GISESD 419
Cdd:COG5635   371 RGEL-PDTRAELYEQFVELLLerwdeqrGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEIlreyLGRRKD 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  420 KAVWLKMQFLQTH-----GNHTV-FYHPTLQSYFAAMFYFLKQDKDICvpvigsipQLLGNMYarGQTQWLQLGTFLFGL 493
Cdd:COG5635   448 AEALLDELLLRTGllverGEGRYsFAHRSFQEYLAARALVEELDEELL--------ELLAEHL--EDPRWREVLLLLAGL 517

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  494 INEqvaalLQPCFGFIQPIYVRQEIICYFKclgQQECNEKLERSQTLFSCLRDSQEERFVRQVVDLLEEITVDISSSDVL 573
Cdd:COG5635   518 LDD-----VKQIKELIDALLARDDAAALAL---AAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALL 589

                         490
                  ....*....|....*...
gi 568945681  574 SVTAYALQKSSKLKKLHL 591
Cdd:COG5635   590 LALLALDLGLAALLLLLL 607
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 387-439 2.72e-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: 2.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568945681   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 7.38e-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: 7.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945681    9 LLKLLQKLSDEEFQRFKELLREEPEKFKlKPISWTKIENSSKESLVTLLNTHY-PGQAWNMMLSLFLQVNREDLS 82
Cdd:cd08321     4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYgEDYAVEVTVEVLRAINQNDLA 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
683-1000 8.53e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.08  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  683 SLFHTLLQLPHLKYLNLYGTYLSmDVTEKL--CAALrcsacrvEELLLGKCGISSkacgiIAISLIN-SKVKHLSLVENP 759
Cdd:COG4886   127 DLPEELANLTNLKELDLSNNQLT-DLPEPLgnLTNL-------KSLDLSNNQLTD-----LPEELGNlTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  760 LKNKGvMSLCEMLKdpscvLQSLMLSYCCLTfiacgHLYEALLSNKHLSLLDLGSNFLEDtgvnlLCEALKDPNctLKEL 839
Cdd:COG4886   194 ITDLP-EPLGNLTN-----LEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD-----LPELGNLTN--LEEL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  840 WLPGCFLTSqcceeISAvLICNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCNLECLGLDLCEFTSdcckDLALALTTCK 919
Cdd:COG4886   256 DLSNNQLTD-----LPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLI----LLLLLTTLLL 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  920 TLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGLDKSAFSEESQTLLQDVEKKNNNLNILHHPWFEAERNKRGTRLVW 999
Cdd:COG4886   326 LLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTL 405


                  .
gi 568945681 1000 N 1000
Cdd:COG4886   406 A 406
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
861-888 1.67e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 1.67e-04
                            10        20
                    ....*....|....*....|....*...
gi 568945681    861 NRNLKTLKLGNNNIQDTGVRQLCEALSH 888
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
799-927 4.43e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945681  799 EALLSNKHLSLLDLGSNFLEDTGVNLlcEALKDpnctLKELWLPGCFLTSqcceeISAVLICNRNLKTLKLGNNNIQDtg 878
Cdd:COG4886   107 EELSNLTNLESLDLSGNQLTDLPEEL--ANLTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-- 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568945681  879 vrqLCEALShpNC-NLECLGLDLCEFTsdcckDLALALTTCKTLNSLNLD 927
Cdd:COG4886   174 ---LPEELG--NLtNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLS 213
 
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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