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Conserved domains on  [gi|194018482|ref|NP_604393|]
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NACHT, LRR and PYD domains-containing protein 4 [Homo sapiens]

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 ...
 149-318 6.94e-53

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: 182.12  E-value: 6.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  149 RTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDrFLYTFYFCCRELRELPP-TSLADLISREWPDPAAPITE----IVSQP 223
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  224 ERLLFVIDSFEELQGGLNEPDSDLcgdlmekrPVQVLLSSLLRKKMLPEASLLIAIKPVCPKELRDQVTISEIYQPRGFN 303
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 194018482  304 ESDRLVYFCCFFKDP 318
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-92 5.08e-40

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: 142.38  E-value: 5.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  11 LMWYLEELKKEEFRKFKEHLKQMTLQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLCMKVMR 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 194018482  91 ER 92
Cdd:cd08320   81 EM 82
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 724-957 1.64e-32

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: 129.01  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 724 NVKELALVNCHLSPIDCEVLAGLLTNNKKLTYLNVSCNQL---DTGVPLLCEALCSpDTVLVYLMLAFCHLSEQCCEYIs 800
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 801 EMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHPDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVG 880
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018482 881 VQLLCRALTHtDCRLEILGLEECGLTSTCCKDLASVLTCSKTLQQLNLTLNTLDHTGVVVLCEALRHPECALQVLGL 957
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-568 1.66e-27

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: 108.15  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  452 HVCIQEFCAALFYLLKSHLDHPHPA-----VRCVQEL--LVANFEKARRAHWIFLGCFLTGLLNKKEQEKLDAFFGFQLS 524
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLkeffgLRKRESLksLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194018482  525 QEIKQQIHQCLKSLGERgnPQGQVDSLAIFYCLFEMQDPAFVKQ 568
Cdd:pfam17776  81 SEIKQELLQWIKSLIQK--ELSSERFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 395-450 5.01e-12

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 61.43  E-value: 5.01e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482  395 QLKALCSLAAEGMWTDTFEFCEDDLRRNGVVDADIPALLGTKILLKYGERESSYVF 450
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 630-733 3.23e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 630 ICSVLTTSGHLRELQVQDSTLSESTFVTWCNQLRHPSCRLQKLGINNVSFSGQSVL-LFEVLFYQPDLKYLSFTLTKLSR 708
Cdd:cd00116  213 LAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKdLAEVLAEKESLLELDLRGNKFGE 292

                         90       100
                 ....*....|....*....|....*
gi 194018482 709 DDIRSLCDALNYPAGNVKELALVNC 733
Cdd:cd00116  293 EGAQLLAESLLEPGNELESLWVKDD 317
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 149-318 6.94e-53

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: 182.12  E-value: 6.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  149 RTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDrFLYTFYFCCRELRELPP-TSLADLISREWPDPAAPITE----IVSQP 223
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  224 ERLLFVIDSFEELQGGLNEPDSDLcgdlmekrPVQVLLSSLLRKKMLPEASLLIAIKPVCPKELRDQVTISEIYQPRGFN 303
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 194018482  304 ESDRLVYFCCFFKDP 318
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-92 5.08e-40

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: 142.38  E-value: 5.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  11 LMWYLEELKKEEFRKFKEHLKQMTLQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLCMKVMR 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 194018482  91 ER 92
Cdd:cd08320   81 EM 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 724-957 1.64e-32

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: 129.01  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 724 NVKELALVNCHLSPIDCEVLAGLLTNNKKLTYLNVSCNQL---DTGVPLLCEALCSpDTVLVYLMLAFCHLSEQCCEYIs 800
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 801 EMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHPDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVG 880
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018482 881 VQLLCRALTHtDCRLEILGLEECGLTSTCCKDLASVLTCSKTLQQLNLTLNTLDHTGVVVLCEALRHPECALQVLGL 957
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 2.08e-30

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: 114.61  E-value: 2.08e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482   10 GLMWYLEELKKEEFRKFKEHLKQMTlQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLC 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-568 1.66e-27

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: 108.15  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  452 HVCIQEFCAALFYLLKSHLDHPHPA-----VRCVQEL--LVANFEKARRAHWIFLGCFLTGLLNKKEQEKLDAFFGFQLS 524
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLkeffgLRKRESLksLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194018482  525 QEIKQQIHQCLKSLGERgnPQGQVDSLAIFYCLFEMQDPAFVKQ 568
Cdd:pfam17776  81 SEIKQELLQWIKSLIQK--ELSSERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 676-945 2.67e-27

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: 116.04  E-value: 2.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 676 NVSFSGQSVLLFEVLFYQPDLKYLsftltklsrddIRSLcdaLNYPAGNVKELALVNCHLSPIDCEVLAGLLTNNKkLTY 755
Cdd:COG5238  120 RRIMAKTLEDSLILYLALPRRINL-----------IQVL---KDPLGGNAVHLLGLAARLGLLAAISMAKALQNNS-VET 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 756 LNVSCNQL-DTGVPLLCEALCSPDTVLVyLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHP 834
Cdd:COG5238  185 VYLGCNQIgDEGIEELAEALTQNTTVTT-LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 835 DCcLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDcRLEILGLEECGLTSTCCKDLA 914
Cdd:COG5238  264 TT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALA 341

                        250       260       270
                 ....*....|....*....|....*....|.
gi 194018482 915 SVLTCSKTLQQLNLTLNTLDHTGVVVLCEAL 945
Cdd:COG5238  342 KALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
149-514 1.64e-15

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 81.39  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 149 RTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDRFLyTFYFCCRELRElpPTSLADLISREWPDPAAPITEIVS---QPER 225
Cdd:COG5635  181 KRLLILGEPGSGKTTLLRYLALELAERYLDAEDPI-PILIELRDLAE--EASLEDLLAEALEKRGGEPEDALErllRNGR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 226 LLFVIDSFEELqgglnePDSDLCGDLMEKrpvqvlLSSLLRKkmLPEASLLIAikpvCPKELRDQVTIS--EIYQPRGFN 303
Cdd:COG5635  258 LLLLLDGLDEV------PDEADRDEVLNQ------LRRFLER--YPKARVIIT----SRPEGYDSSELEgfEVLELAPLS 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 304 ESDRLVYFCCFFKDPKRAMEAF-NLVRESEQLFSICQIPLLCWILCTSLKQemqkGKDLAltcQSTTSVYSSFVFNLFT- 381
Cdd:COG5635  320 DEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRE----RGELP---DTRAELYEQFVELLLEr 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 382 ----PEGAEGPTPQTQHQLKALCSLAAEGMWTDTFEFCEDDLRR------NGVVDADI---PALLGTKILLKYGEREssY 448
Cdd:COG5635  393 wdeqRGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKDAEAlldELLLRTGLLVERGEGR--Y 470

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482 449 VFLHVCIQEFCAALFylLKSHLDhphpavRCVQELLVANFEkarRAHWIFLGCFLTGLLNKKEQEK 514
Cdd:COG5635  471 SFAHRSFQEYLAARA--LVEELD------EELLELLAEHLE---DPRWREVLLLLAGLLDDVKQIK 525
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 395-450 5.01e-12

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 61.43  E-value: 5.01e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482  395 QLKALCSLAAEGMWTDTFEFCEDDLRRNGVVDADIPALLGTKILLKYGERESSYVF 450
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
806-833 2.33e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 36.23  E-value: 2.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 194018482   806 NKSVRYLDLSANVLKDEGLKTLCEALKH 833
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 147-279 2.82e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482   147 QPRTVIIQGPQGIGKTTLLMKLMmawsdnKIFRDRFLYTFYFCCRELRELPPTSLADLISREWPDP------AAPITEIV 220
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrLRLALALA 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 194018482   221 SQPERLLFVIDsfeelqgglnEPDSdLCGDLMEKRPVQVLLSSLLRKKMLPEASLLIAI 279
Cdd:smart00382  75 RKLKPDVLILD----------EITS-LLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
LRR_6 pfam13516
Leucine Rich repeat;
862-885 3.15e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.67  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|....
gi 194018482  862 SNQNLKILQIGCNEIGDVGVQLLC 885
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 630-733 3.23e-03

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: 40.80  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 630 ICSVLTTSGHLRELQVQDSTLSESTFVTWCNQLRHPSCRLQKLGINNVSFSGQSVL-LFEVLFYQPDLKYLSFTLTKLSR 708
Cdd:cd00116  213 LAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKdLAEVLAEKESLLELDLRGNKFGE 292

                         90       100
                 ....*....|....*....|....*
gi 194018482 709 DDIRSLCDALNYPAGNVKELALVNC 733
Cdd:cd00116  293 EGAQLLAESLLEPGNELESLWVKDD 317
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 149-318 6.94e-53

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: 182.12  E-value: 6.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  149 RTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDrFLYTFYFCCRELRELPP-TSLADLISREWPDPAAPITE----IVSQP 223
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  224 ERLLFVIDSFEELQGGLNEPDSDLcgdlmekrPVQVLLSSLLRKKMLPEASLLIAIKPVCPKELRDQVTISEIYQPRGFN 303
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 194018482  304 ESDRLVYFCCFFKDP 318
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-92 5.08e-40

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: 142.38  E-value: 5.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  11 LMWYLEELKKEEFRKFKEHLKQMTLQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLCMKVMR 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 194018482  91 ER 92
Cdd:cd08320   81 EM 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 724-957 1.64e-32

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: 129.01  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 724 NVKELALVNCHLSPIDCEVLAGLLTNNKKLTYLNVSCNQL---DTGVPLLCEALCSpDTVLVYLMLAFCHLSEQCCEYIs 800
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 801 EMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHPDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVG 880
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018482 881 VQLLCRALTHtDCRLEILGLEECGLTSTCCKDLASVLTCSKTLQQLNLTLNTLDHTGVVVLCEALRHPECALQVLGL 957
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 686-957 2.98e-32

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: 128.24  E-value: 2.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 686 LFEVLFYQPDLKYLSFTLTKLSRDD--IRSLCDALNYPAGnVKELALVNCHLSPIDCEVLAGLLTNNK-KLTYLNvSCNQ 762
Cdd:cd00116   43 LASALRPQPSLKELCLSLNETGRIPrgLQSLLQGLTKGCG-LQELDLSDNALGPDGCGVLESLLRSSSlQELKLN-NNGL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 763 LDTGVPLLCEALCSPDTVLVYLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHpDCCLDSLC 842
Cdd:cd00116  121 GDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 843 LVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDCRLEILGLEECGLTSTCCKDLASVLTCSKT 922
Cdd:cd00116  200 LNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKES 279

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 194018482 923 LQQLNLTLNTLDHTGVVVLCEALRHPECALQVLGL 957
Cdd:cd00116  280 LLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 2.08e-30

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: 114.61  E-value: 2.08e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482   10 GLMWYLEELKKEEFRKFKEHLKQMTlQLELKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLC 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-568 1.66e-27

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: 108.15  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482  452 HVCIQEFCAALFYLLKSHLDHPHPA-----VRCVQEL--LVANFEKARRAHWIFLGCFLTGLLNKKEQEKLDAFFGFQLS 524
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLkeffgLRKRESLksLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194018482  525 QEIKQQIHQCLKSLGERgnPQGQVDSLAIFYCLFEMQDPAFVKQ 568
Cdd:pfam17776  81 SEIKQELLQWIKSLIQK--ELSSERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 676-945 2.67e-27

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: 116.04  E-value: 2.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 676 NVSFSGQSVLLFEVLFYQPDLKYLsftltklsrddIRSLcdaLNYPAGNVKELALVNCHLSPIDCEVLAGLLTNNKkLTY 755
Cdd:COG5238  120 RRIMAKTLEDSLILYLALPRRINL-----------IQVL---KDPLGGNAVHLLGLAARLGLLAAISMAKALQNNS-VET 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 756 LNVSCNQL-DTGVPLLCEALCSPDTVLVyLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHP 834
Cdd:COG5238  185 VYLGCNQIgDEGIEELAEALTQNTTVTT-LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 835 DCcLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDcRLEILGLEECGLTSTCCKDLA 914
Cdd:COG5238  264 TT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALA 341

                        250       260       270
                 ....*....|....*....|....*....|.
gi 194018482 915 SVLTCSKTLQQLNLTLNTLDHTGVVVLCEAL 945
Cdd:COG5238  342 KALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 672-976 5.37e-27

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: 115.27  E-value: 5.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 672 LGINNVSFSG--QSVLLFEVLFYQPDLKYLSFTLTKLSRDDI-----RSLCDALNYPAgNVKELALVNCHLSPIDCEVLA 744
Cdd:COG5238  151 LGGNAVHLLGlaARLGLLAAISMAKALQNNSVETVYLGCNQIgdegiEELAEALTQNT-TVTTLWLKRNPIGDEGAEILA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 745 GLLTNNKKLTYLNVSCNQL-DTGVPLLCEALCSPDTVlVYLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEG 823
Cdd:COG5238  230 EALKGNKSLTTLDLSNNQIgDEGVIALAEALKNNTTV-ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 824 LKTLCEALKHpDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRAL-THTdcrleilglee 902
Cdd:COG5238  309 AIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNT----------- 376

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018482 903 cgltstcckdlasvltcskTLQQLNLTLNTLDHTGVVVLCEALRHPEcaLQVLGLRKTDFDEETQALLTAEEER 976
Cdd:COG5238  377 -------------------TLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILDGNLIGAEAQQRLEQLLER 429
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 667-903 1.82e-25

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: 108.21  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 667 CRLQKLGINNVSFSGQSVLLFEVLFYQPDLKYLSFTLTKLSRDDIRSLCDALNYPAGNVKELALVNCHLSPIDCEVLAGL 746
Cdd:cd00116   81 CGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 747 LTNNKKLTYLNVSCNQL-DTGVPLLCEALCSpDTVLVYLMLAFCHLSEQCCEYISEMLLRNKSVRYLDLSANVLKDEGLK 825
Cdd:cd00116  161 LRANRDLKELNLANNGIgDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAA 239

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194018482 826 TLCEALKHPDCCLDSLCLVKCFITAAGCEDLASALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDCRLEILGLEEC 903
Cdd:cd00116  240 ALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 779-987 1.48e-16

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: 83.30  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 779 TVLVYLMLAFCHLSEQCCEYIS-EMLLRNKSVRYLDLSANVLKDEGLKTLCEALKHPDCcLDSLCLVKCFITAAGCEDLA 857
Cdd:COG5238  151 LGGNAVHLLGLAARLGLLAAISmAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTT-VTTLWLKRNPIGDEGAEILA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 858 SALISNQNLKILQIGCNEIGDVGVQLLCRALTHTDcRLEILGLEECGLTSTCCKDLASVLTCSKTLQQLNLTLNTLDHTG 937
Cdd:COG5238  230 EALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194018482 938 VVVLCEALRHPEcALQVLGLRKTDF-DEETQALLTAEEErNPNLTITDDCD 987
Cdd:COG5238  309 AIALAEGLQGNK-TLHTLNLAYNGIgAQGAIALAKALQE-NTTLHSLDLSD 357
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-84 3.42e-16

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: 74.10  E-value: 3.42e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018482  11 LMWYLEELKKEEFRKFKEHLKQMTLQLElKQIPWTEVKKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDL 84
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
149-514 1.64e-15

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 81.39  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 149 RTVIIQGPQGIGKTTLLMKLMMAWSDNKIFRDRFLyTFYFCCRELRElpPTSLADLISREWPDPAAPITEIVS---QPER 225
Cdd:COG5635  181 KRLLILGEPGSGKTTLLRYLALELAERYLDAEDPI-PILIELRDLAE--EASLEDLLAEALEKRGGEPEDALErllRNGR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 226 LLFVIDSFEELqgglnePDSDLCGDLMEKrpvqvlLSSLLRKkmLPEASLLIAikpvCPKELRDQVTIS--EIYQPRGFN 303
Cdd:COG5635  258 LLLLLDGLDEV------PDEADRDEVLNQ------LRRFLER--YPKARVIIT----SRPEGYDSSELEgfEVLELAPLS 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 304 ESDRLVYFCCFFKDPKRAMEAF-NLVRESEQLFSICQIPLLCWILCTSLKQemqkGKDLAltcQSTTSVYSSFVFNLFT- 381
Cdd:COG5635  320 DEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRE----RGELP---DTRAELYEQFVELLLEr 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 382 ----PEGAEGPTPQTQHQLKALCSLAAEGMWTDTFEFCEDDLRR------NGVVDADI---PALLGTKILLKYGEREssY 448
Cdd:COG5635  393 wdeqRGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKDAEAlldELLLRTGLLVERGEGR--Y 470

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482 449 VFLHVCIQEFCAALFylLKSHLDhphpavRCVQELLVANFEkarRAHWIFLGCFLTGLLNKKEQEK 514
Cdd:COG5635  471 SFAHRSFQEYLAARA--LVEELD------EELLELLAEHLE---DPRWREVLLLLAGLLDDVKQIK 525
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 395-450 5.01e-12

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 61.43  E-value: 5.01e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194018482  395 QLKALCSLAAEGMWTDTFEFCEDDLRRNGVVDADIPALLGTKILLKYGERESSYVF 450
Cdd:pfam17779   2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 11-85 2.66e-06

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 45.76  E-value: 2.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194018482  11 LMWYLEELKKEEFRKFKEHLKQmTLQLELKQIPwtevkKASREELANLLIKHYEEQQAWNITLRIFQKMDRKDLC 85
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLAS-ELKLTRKMQE-----EYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLA 69
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
724-933 6.78e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.38  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 724 NVKELALVNCHLSPIDCEvlaglLTNNKKLTYLNVSCNQLDTgvplLCEALcSPDTVLVYLMLAFCHLSEqcceyISEML 803
Cdd:COG4886  114 NLESLDLSGNQLTDLPEE-----LANLTNLKELDLSNNQLTD----LPEPL-GNLTNLKSLDLSNNQLTD-----LPEEL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 804 LRNKSVRYLDLSANVLkdeglktlcealkhpdccldslclvkcfitaagcEDLASALISNQNLKILQIGCNEIGDVGVQL 883
Cdd:COG4886  179 GNLTNLKELDLSNNQI----------------------------------TDLPEPLGNLTNLEELDLSGNQLTDLPEPL 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 194018482 884 lcRALThtdcRLEILGLEECGLTstcckDLASVLTCSKtLQQLNLTLNTL 933
Cdd:COG4886  225 --ANLT----NLETLDLSNNQLT-----DLPELGNLTN-LEELDLSNNQL 262
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
806-833 2.33e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 36.23  E-value: 2.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 194018482   806 NKSVRYLDLSANVLKDEGLKTLCEALKH 833
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 130-208 2.60e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.79  E-value: 2.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194018482  130 EECDHLDRLFAPKEAGkQPRTVIIQGPQGIGKTTLLMKLMmawsdnKIFRDRFLYTFYFCCRELreLPPTSLADLISRE 208
Cdd:pfam13191   7 EELEQLLDALDRVRSG-RPPSVLLTGEAGTGKTTLLRELL------RALERDGGYFLRGKCDEN--LPYSPLLEALTRE 76
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 147-279 2.82e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482   147 QPRTVIIQGPQGIGKTTLLMKLMmawsdnKIFRDRFLYTFYFCCRELRELPPTSLADLISREWPDP------AAPITEIV 220
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrLRLALALA 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 194018482   221 SQPERLLFVIDsfeelqgglnEPDSdLCGDLMEKRPVQVLLSSLLRKKMLPEASLLIAI 279
Cdd:smart00382  75 RKLKPDVLILD----------EITS-LLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
LRR_6 pfam13516
Leucine Rich repeat;
862-885 3.15e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.67  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|....
gi 194018482  862 SNQNLKILQIGCNEIGDVGVQLLC 885
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 630-733 3.23e-03

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: 40.80  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018482 630 ICSVLTTSGHLRELQVQDSTLSESTFVTWCNQLRHPSCRLQKLGINNVSFSGQSVL-LFEVLFYQPDLKYLSFTLTKLSR 708
Cdd:cd00116  213 LAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKdLAEVLAEKESLLELDLRGNKFGE 292

                         90       100
                 ....*....|....*....|....*
gi 194018482 709 DDIRSLCDALNYPAGNVKELALVNC 733
Cdd:cd00116  293 EGAQLLAESLLEPGNELESLWVKDD 317
 
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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