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Conserved domains on  [gi|27369660|ref|NP_766069|]
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NACHT, LRR and PYD domains-containing protein 4B [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 145-311 1.06e-33

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: 127.04  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   145 VVLQGVAGIGKTILLKNLMIVWSEGLVFQnKFSYIFYFCCHDVKQLQTA-SLADLISREWPSPSAPMEE----ILSQPEK 219
Cdd:pfam05729   3 VILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   220 LLFIIDSLEGMEWnVTQQDSQLCyncmekqPVNVLLSSLLRKKILPESSLLISTSCETFKDLKDWIEYTNVRTITGFKEN 299
Cdd:pfam05729  82 LLLILDGLDELVS-DLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|..
gi 27369660   300 NINMCFHSLFQD 311
Cdd:pfam05729 154 DRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 1.51e-31

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: 118.11  E-value: 1.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660  10 FIWYWKELNKIEFMYFKELLIHEILQMGLKQISWTEVKEASREDLAILLVKHCDGNQAWDTTFRVFQMIGRNVITNRATG 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 27369660  90 EIAA 93
Cdd:cd08320  81 EMNE 84
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 601-834 1.25e-23

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: 102.82  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 601 QNVLNEElgqRGKllilwhQICSVFLRNKDIKTL--RIEDTIFNEPVFKIFYSYLKNSSCiLKTLVAYNVSFLCDKRLFL 678
Cdd:cd00116  32 GNTLGEE---AAK------ALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCG-LQELDLSDNALGPDGCGVL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 679 E-LIQSYNLEELYLRGTFLSHSDVEMLCDILNQAECNIRILDLANCSLCEHSWDYLSDVLRQNKSLRYLNISYNNLKDEG 757
Cdd:cd00116 102 EsLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660 758 LKALCRALTlPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKAMKDQTCTLYELKL 834
Cdd:cd00116 182 IRALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 446-562 8.21e-19

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: 83.11  E-value: 8.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   446 HPSVQEFCAAMFYLLHSEMDHSCQGVYFIETFLFTFLNKI--------KKQWVFLGCFFFGLLHETEQEKLEAFFGYHLS 517
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLldkalkskNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 27369660   518 KELRRQLFLWLELLLDTLHPDVKKINtmkFFYCLFEMEEEVFVQS 562
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSERFLN---LFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-444 8.59e-09

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: 52.18  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660   388 DLLDNLCFLAVEGMWTDISVFNEEALRRNGIMDSDIPTLLDIGILEQSRESENSYIF 444
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 145-311 1.06e-33

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: 127.04  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   145 VVLQGVAGIGKTILLKNLMIVWSEGLVFQnKFSYIFYFCCHDVKQLQTA-SLADLISREWPSPSAPMEE----ILSQPEK 219
Cdd:pfam05729   3 VILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   220 LLFIIDSLEGMEWnVTQQDSQLCyncmekqPVNVLLSSLLRKKILPESSLLISTSCETFKDLKDWIEYTNVRTITGFKEN 299
Cdd:pfam05729  82 LLLILDGLDELVS-DLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|..
gi 27369660   300 NINMCFHSLFQD 311
Cdd:pfam05729 154 DRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 1.51e-31

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: 118.11  E-value: 1.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660  10 FIWYWKELNKIEFMYFKELLIHEILQMGLKQISWTEVKEASREDLAILLVKHCDGNQAWDTTFRVFQMIGRNVITNRATG 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 27369660  90 EIAA 93
Cdd:cd08320  81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 601-834 1.25e-23

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: 102.82  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 601 QNVLNEElgqRGKllilwhQICSVFLRNKDIKTL--RIEDTIFNEPVFKIFYSYLKNSSCiLKTLVAYNVSFLCDKRLFL 678
Cdd:cd00116  32 GNTLGEE---AAK------ALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCG-LQELDLSDNALGPDGCGVL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 679 E-LIQSYNLEELYLRGTFLSHSDVEMLCDILNQAECNIRILDLANCSLCEHSWDYLSDVLRQNKSLRYLNISYNNLKDEG 757
Cdd:cd00116 102 EsLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660 758 LKALCRALTlPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKAMKDQTCTLYELKL 834
Cdd:cd00116 182 IRALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-81 1.97e-19

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: 83.02  E-value: 1.97e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660    12 WYWKELNKIEFMYFKELLIHEIlQMGLKQISWTEVKEASREDLAILLVKHCDGNQAWDTTFRVFQMIGRN 81
Cdd:pfam02758   4 WYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLK 72
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 446-562 8.21e-19

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: 83.11  E-value: 8.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   446 HPSVQEFCAAMFYLLHSEMDHSCQGVYFIETFLFTFLNKI--------KKQWVFLGCFFFGLLHETEQEKLEAFFGYHLS 517
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLldkalkskNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 27369660   518 KELRRQLFLWLELLLDTLHPDVKKINtmkFFYCLFEMEEEVFVQS 562
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSERFLN---LFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 585-855 9.58e-15

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: 77.52  E-value: 9.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 585 YCLSHGSALTDFSISAQNVLNEELGQRGKLLIlwhqiCSVFLRNKDIKTLRIEDTIFNEPVFKIFYSYLK-NSSciLKTL 663
Cdd:COG5238 169 AAISMAKALQNNSVETVYLGCNQIGDEGIEEL-----AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKgNKS--LTTL 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 664 VAYNVSFLCD--KRLFLELIQSYNLEELYLRGTFLSHSDVEMLCDILnQAECNIRILDLANCSLCEHSWDYLSDVLRQNK 741
Cdd:COG5238 242 DLSNNQIGDEgvIALAEALKNNTTVETLYLSGNQIGAEGAIALAKAL-QGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK 320

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 742 SLRYLNISYNNLKDEGLKALCRALTlPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKA 821
Cdd:COG5238 321 TLHTLNLAYNGIGAQGAIALAKALQ-ENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDA 399

                       250       260       270
                ....*....|....*....|....*....|....
gi 27369660 822 MkdQTCTLYELKLRMADFDSDSQEFLLSEMERNK 855
Cdd:COG5238 400 L--QTNRLHTLILDGNLIGAEAQQRLEQLLERIK 431
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-444 8.59e-09

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: 52.18  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660   388 DLLDNLCFLAVEGMWTDISVFNEEALRRNGIMDSDIPTLLDIGILEQSRESENSYIF 444
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
139-507 5.08e-08

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 56.74  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 139 ENNPKMVVLQGVAGIGKTILLKNLMIVWSEGLVFQNKFsYIFYFCCHDVKqlQTASLADLISREWPSPSAPMEEILS--- 215
Cdd:COG5635 177 EAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErll 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 216 QPEKLLFIIDSL-EgmewnVTQQDSQlcyncmeKQPVNvLLSSLLRKkiLPESSLLIsTSCETFKDlKDWIEYTNVRTIT 294
Cdd:COG5635 254 RNGRLLLLLDGLdE-----VPDEADR-------DEVLN-QLRRFLER--YPKARVII-TSRPEGYD-SSELEGFEVLELA 316

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 295 GFKENNINMCFHSLFQDRNIAQEAF-SLIRENEQLFTVCQAPVVCYMVATCLKNEIESGKDPVSICRR-TTSLYTTHILN 372
Cdd:COG5635 317 PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAELYEQfVELLLERWDEQ 396

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 373 lfiPHNAQNPSNNSEDLLDNLCFLAVEGMWTDISVFNEEALRRngIMDSDIPTLLDIG-----ILEQS----RESENSYI 443
Cdd:COG5635 397 ---RGLTIYRELSREELRELLSELALAMQENGRTEFAREELEE--ILREYLGRRKDAEalldeLLLRTgllvERGEGRYS 471

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369660 444 FLHPSVQEFCAAMFYLLHSEMDhscqgvyfIETFLFTFLNKIKKQWVFLgcFFFGLLHETEQEK 507
Cdd:COG5635 472 FAHRSFQEYLAARALVEELDEE--------LLELLAEHLEDPRWREVLL--LLAGLLDDVKQIK 525
LRR_6 pfam13516
Leucine Rich repeat;
739-762 3.07e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 38.37  E-value: 3.07e-04
                          10        20
                  ....*....|....*....|....
gi 27369660   739 QNKSLRYLNISYNNLKDEGLKALC 762
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
740-766 3.13e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.54  E-value: 3.13e-04
                           10        20
                   ....*....|....*....|....*..
gi 27369660    740 NKSLRYLNISYNNLKDEGLKALCRALT 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALK 27
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 145-311 1.06e-33

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: 127.04  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   145 VVLQGVAGIGKTILLKNLMIVWSEGLVFQnKFSYIFYFCCHDVKQLQTA-SLADLISREWPSPSAPMEE----ILSQPEK 219
Cdd:pfam05729   3 VILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELPER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   220 LLFIIDSLEGMEWnVTQQDSQLCyncmekqPVNVLLSSLLRKKILPESSLLISTSCETFKDLKDWIEYTNVRTITGFKEN 299
Cdd:pfam05729  82 LLLILDGLDELVS-DLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|..
gi 27369660   300 NINMCFHSLFQD 311
Cdd:pfam05729 154 DRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-93 1.51e-31

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: 118.11  E-value: 1.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660  10 FIWYWKELNKIEFMYFKELLIHEILQMGLKQISWTEVKEASREDLAILLVKHCDGNQAWDTTFRVFQMIGRNVITNRATG 89
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ....
gi 27369660  90 EIAA 93
Cdd:cd08320  81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 601-834 1.25e-23

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: 102.82  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 601 QNVLNEElgqRGKllilwhQICSVFLRNKDIKTL--RIEDTIFNEPVFKIFYSYLKNSSCiLKTLVAYNVSFLCDKRLFL 678
Cdd:cd00116  32 GNTLGEE---AAK------ALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCG-LQELDLSDNALGPDGCGVL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 679 E-LIQSYNLEELYLRGTFLSHSDVEMLCDILNQAECNIRILDLANCSLCEHSWDYLSDVLRQNKSLRYLNISYNNLKDEG 757
Cdd:cd00116 102 EsLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660 758 LKALCRALTlPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKAMKDQTCTLYELKL 834
Cdd:cd00116 182 IRALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-81 1.97e-19

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: 83.02  E-value: 1.97e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660    12 WYWKELNKIEFMYFKELLIHEIlQMGLKQISWTEVKEASREDLAILLVKHCDGNQAWDTTFRVFQMIGRN 81
Cdd:pfam02758   4 WYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLK 72
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 446-562 8.21e-19

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: 83.11  E-value: 8.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660   446 HPSVQEFCAAMFYLLHSEMDHSCQGVYFIETFLFTFLNKI--------KKQWVFLGCFFFGLLHETEQEKLEAFFGYHLS 517
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLldkalkskNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 27369660   518 KELRRQLFLWLELLLDTLHPDVKKINtmkFFYCLFEMEEEVFVQS 562
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSERFLN---LFHCLYELQDESFVKE 122
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 653-821 1.51e-16

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: 81.63  E-value: 1.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 653 LKNSSCILKTLVAY--NVSFLCDKRLFLELIQSYNLEELYLRGTFLSHSDVEMLCDILnQAECNIRILDLANCSLCEHSW 730
Cdd:cd00116 132 LKDLPPALEKLVLGrnRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGA 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 731 DYLSDVLRQNKSLRYLNISYNNLKDEGLKALCRALTLPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSL 810
Cdd:cd00116 211 SALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290

                       170
                ....*....|.
gi 27369660 811 GFSGLFVLCKA 821
Cdd:cd00116 291 GEEGAQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 686-835 5.64e-16

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: 79.71  E-value: 5.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 686 LEELYLRGTFLSHSDVEMLCDILN-QAECNIRILDLANCSLCEHSWDYLSDvLRQNKSLRYLNISYNNLKDEGLKALCRA 764
Cdd:cd00116  53 LKELCLSLNETGRIPRGLQSLLQGlTKGCGLQELDLSDNALGPDGCGVLES-LLRSSSLQELKLNNNGLGDRGLRLLAKG 131

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369660 765 LTLPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKAMKDQtCTLYELKLR 835
Cdd:cd00116 132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLN 201
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 585-855 9.58e-15

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: 77.52  E-value: 9.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 585 YCLSHGSALTDFSISAQNVLNEELGQRGKLLIlwhqiCSVFLRNKDIKTLRIEDTIFNEPVFKIFYSYLK-NSSciLKTL 663
Cdd:COG5238 169 AAISMAKALQNNSVETVYLGCNQIGDEGIEEL-----AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKgNKS--LTTL 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 664 VAYNVSFLCD--KRLFLELIQSYNLEELYLRGTFLSHSDVEMLCDILnQAECNIRILDLANCSLCEHSWDYLSDVLRQNK 741
Cdd:COG5238 242 DLSNNQIGDEgvIALAEALKNNTTVETLYLSGNQIGAEGAIALAKAL-QGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK 320

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 742 SLRYLNISYNNLKDEGLKALCRALTlPNSALHSLSLEACQLTGACCKDLASTFTRYKCLRRINLAKNSLGFSGLFVLCKA 821
Cdd:COG5238 321 TLHTLNLAYNGIGAQGAIALAKALQ-ENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDA 399

                       250       260       270
                ....*....|....*....|....*....|....
gi 27369660 822 MkdQTCTLYELKLRMADFDSDSQEFLLSEMERNK 855
Cdd:COG5238 400 L--QTNRLHTLILDGNLIGAEAQQRLEQLLERIK 431
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-444 8.59e-09

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: 52.18  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 27369660   388 DLLDNLCFLAVEGMWTDISVFNEEALRRNGIMDSDIPTLLDIGILEQSRESENSYIF 444
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
139-507 5.08e-08

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 56.74  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 139 ENNPKMVVLQGVAGIGKTILLKNLMIVWSEGLVFQNKFsYIFYFCCHDVKqlQTASLADLISREWPSPSAPMEEILS--- 215
Cdd:COG5635 177 EAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErll 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 216 QPEKLLFIIDSL-EgmewnVTQQDSQlcyncmeKQPVNvLLSSLLRKkiLPESSLLIsTSCETFKDlKDWIEYTNVRTIT 294
Cdd:COG5635 254 RNGRLLLLLDGLdE-----VPDEADR-------DEVLN-QLRRFLER--YPKARVII-TSRPEGYD-SSELEGFEVLELA 316

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 295 GFKENNINMCFHSLFQDRNIAQEAF-SLIRENEQLFTVCQAPVVCYMVATCLKNEIESGKDPVSICRR-TTSLYTTHILN 372
Cdd:COG5635 317 PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAELYEQfVELLLERWDEQ 396

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 373 lfiPHNAQNPSNNSEDLLDNLCFLAVEGMWTDISVFNEEALRRngIMDSDIPTLLDIG-----ILEQS----RESENSYI 443
Cdd:COG5635 397 ---RGLTIYRELSREELRELLSELALAMQENGRTEFAREELEE--ILREYLGRRKDAEalldeLLLRTgllvERGEGRYS 471

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369660 444 FLHPSVQEFCAAMFYLLHSEMDhscqgvyfIETFLFTFLNKIKKQWVFLgcFFFGLLHETEQEK 507
Cdd:COG5635 472 FAHRSFQEYLAARALVEELDEE--------LLELLAEHLEDPRWREVLL--LLAGLLDDVKQIK 525
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 620-782 8.21e-07

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: 51.97  E-value: 8.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 620 QICSVFLRNKDIKTLRIEDTIFNEPVFKIFYSYLKnSSCILKTLVAYNVSFLCDKRLFLE--LIQSYNLEELYLRGTFLS 697
Cdd:cd00116 156 ALAKALRANRDLKELNLANNGIGDAGIRALAEGLK-ANCNLEVLDLNNNGLTDEGASALAetLASLKSLEVLNLGDNNLT 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 698 HSDVEMLCDILNQAECNIRILDLANCSLCEHSWDYLSDVLRQNKSLRYLNISYNNLKDEGLKALCRALTLPNSALHSLSL 777
Cdd:cd00116 235 DAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314


                ....*
gi 27369660 778 EACQL 782
Cdd:cd00116 315 KDDSF 319
LRR_6 pfam13516
Leucine Rich repeat;
739-762 3.07e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 38.37  E-value: 3.07e-04
                          10        20
                  ....*....|....*....|....
gi 27369660   739 QNKSLRYLNISYNNLKDEGLKALC 762
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
740-766 3.13e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.54  E-value: 3.13e-04
                           10        20
                   ....*....|....*....|....*..
gi 27369660    740 NKSLRYLNISYNNLKDEGLKALCRALT 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 730-835 9.55e-04

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: 42.34  E-value: 9.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 730 WDYLSDVLRQNKSLRylnISYNNLKDEGLKALCRALTLPNSALH-SLSLEACQLTGACCKDLASTFTRYKCLRRINLAKN 808
Cdd:cd00116  15 ATELLPKLLCLQVLR---LEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDN 91

                        90       100
                ....*....|....*....|....*....
gi 27369660 809 SLGFSGlfvlCKAMKD--QTCTLYELKLR 835
Cdd:cd00116  92 ALGPDG----CGVLESllRSSSLQELKLN 116
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
685-810 2.43e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 2.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369660 685 NLEELYLRGTFLSHsdvemLCDILNQAEcNIRILDLANCSLCEhswdyLSDVLRQNKSLRYLNISYNNLKD--EGLKALc 762
Cdd:COG4886 160 NLKSLDLSNNQLTD-----LPEELGNLT-NLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTDlpEPLANL- 227

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 27369660 763 raltlpnSALHSLSLEACQLTgacckDLAStFTRYKCLRRINLAKNSL 810
Cdd:COG4886 228 -------TNLETLDLSNNQLT-----DLPE-LGNLTNLEELDLSNNQL 262
 
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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