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Conserved domains on  [gi|452085171|ref|NP_612202|]
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NACHT, LRR and PYD domains-containing protein 6 isoform 1 [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 ...
197-350 1.25e-44

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: 158.24  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERPGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171  273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
501-636 1.28e-21

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: 91.20  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 452085171  571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
31-99 2.95e-21

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: 88.74  E-value: 2.95e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321   13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
35-782 2.63e-17

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 87.17  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  35 KRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRAD-ARDVAAQLQERRLQRLGLGSGTLL 113
Cdd:COG5635   23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALsALLLVLLLLESLLLLLLLLLLLAE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 114 SVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEAMGPAEEPEPGRARRSDThTFNRLFRRDEEGR 193
Cdd:COG5635  103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIE-SLKRLELLEAKKK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 194 RpltVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVdFAFFMPCGELLERPgtrSLADLILDQCPDRGAPVPQM---LAQ 270
Cdd:COG5635  182 R---LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLAEEA---SLEDLLAEALEKRGGEPEDAlerLLR 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 271 PQRLLFILDGADELPalggpeaapctDPFEAASGARVLGGLLSKalLPTALLLVTTRAAA--PGRLQGRlcspQCAEVRG 348
Cdd:COG5635  255 NGRLLLLLDGLDEVP-----------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGydSSELEGF----EVLELAP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 349 FSDKDKKK-YFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRtsktttsVYLLFITSVL 427
Cdd:COG5635  318 LSDEQIEEfLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE-------LYEQFVELLL 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 428 SSAPVADGPRLQGDL------RNLCRLAREGVLGRRAQFAEKELEQL---ELRGSKVQTLFLSKKELPGVL---ETEVTY 495
Cdd:COG5635  391 ERWDEQRGLTIYRELsreelrELLSELALAMQENGRTEFAREELEEIlreYLGRRKDAEALLDELLLRTGLlveRGEGRY 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 496 QFIDQSFQEFLAALsYLLEDGGVPRTAAggvgtLLRGDAQPHSHLVLttRFLFGLLSaeRMRDIERHFGCMVSERVKQEA 575
Cdd:COG5635  471 SFAHRSFQEYLAAR-ALVEELDEELLEL-----LAEHLEDPRWREVL--LLLAGLLD--DVKQIKELIDALLARDDAAAL 540
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 576 LRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMD 655
Cdd:COG5635  541 ALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALAL 620
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 656 VAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLFQAMTDPLCHLSSLTL 735
Cdd:COG5635  621 LLALLLLLLLLLLAELLLLALLALVLLSLLLASRLLLITLLLLAAASAALLLLLLLLLAELLLALLALASLLLLLLLALA 700
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*..
gi 452085171 736 SHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAW 782
Cdd:COG5635  701 LALALLLLAVLLAAALDLLLLLVLLLALLLVLALALSLLLLALALLL 747
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
729-868 1.25e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 48.63  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 729 HLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLawpQCRVQTVRVQLPDPQRG-------L 801
Cdd:COG5238  293 TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL---QENTTLHSLDLSDNQIGdegaialA 369
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 802 QYLVGmlrqSPALTTLDLSGCQLPAPMVTYLCAVLQHQgcGLQTLSLASVELSEQSLQEL-QAVKRAK 868
Cdd:COG5238  370 KYLEG----NTTLRELNLGKNNIGKQGAEALIDALQTN--RLHTLILDGNLIGAEAQQRLeQLLERIK 431
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
197-350 1.25e-44

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: 158.24  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERPGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171  273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
501-636 1.28e-21

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: 91.20  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 452085171  571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
31-99 2.95e-21

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: 88.74  E-value: 2.95e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321   13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
35-782 2.63e-17

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 87.17  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  35 KRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRAD-ARDVAAQLQERRLQRLGLGSGTLL 113
Cdd:COG5635   23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALsALLLVLLLLESLLLLLLLLLLLAE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 114 SVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEAMGPAEEPEPGRARRSDThTFNRLFRRDEEGR 193
Cdd:COG5635  103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIE-SLKRLELLEAKKK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 194 RpltVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVdFAFFMPCGELLERPgtrSLADLILDQCPDRGAPVPQM---LAQ 270
Cdd:COG5635  182 R---LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLAEEA---SLEDLLAEALEKRGGEPEDAlerLLR 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 271 PQRLLFILDGADELPalggpeaapctDPFEAASGARVLGGLLSKalLPTALLLVTTRAAA--PGRLQGRlcspQCAEVRG 348
Cdd:COG5635  255 NGRLLLLLDGLDEVP-----------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGydSSELEGF----EVLELAP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 349 FSDKDKKK-YFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRtsktttsVYLLFITSVL 427
Cdd:COG5635  318 LSDEQIEEfLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE-------LYEQFVELLL 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 428 SSAPVADGPRLQGDL------RNLCRLAREGVLGRRAQFAEKELEQL---ELRGSKVQTLFLSKKELPGVL---ETEVTY 495
Cdd:COG5635  391 ERWDEQRGLTIYRELsreelrELLSELALAMQENGRTEFAREELEEIlreYLGRRKDAEALLDELLLRTGLlveRGEGRY 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 496 QFIDQSFQEFLAALsYLLEDGGVPRTAAggvgtLLRGDAQPHSHLVLttRFLFGLLSaeRMRDIERHFGCMVSERVKQEA 575
Cdd:COG5635  471 SFAHRSFQEYLAAR-ALVEELDEELLEL-----LAEHLEDPRWREVL--LLLAGLLD--DVKQIKELIDALLARDDAAAL 540
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 576 LRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMD 655
Cdd:COG5635  541 ALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALAL 620
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 656 VAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLFQAMTDPLCHLSSLTL 735
Cdd:COG5635  621 LLALLLLLLLLLLAELLLLALLALVLLSLLLASRLLLITLLLLAAASAALLLLLLLLLAELLLALLALASLLLLLLLALA 700
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*..
gi 452085171 736 SHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAW 782
Cdd:COG5635  701 LALALLLLAVLLAAALDLLLLLVLLLALLLVLALALSLLLLALALLL 747
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
30-95 1.10e-16

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: 75.32  E-value: 1.10e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 452085171   30 SQEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAA 95
Cdd:pfam02758  10 SEEEFKKFKSLLEDEPEEGlRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
545-872 7.24e-14

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 73.54  E-value: 7.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 545 RFLFGLLSAERMRDIERHFGCMVSERVKQEALRWvqgqgqgcpgvapevtEGAKGLEDTEEPEEEEegeepnypLELLYC 624
Cdd:cd00116    4 SLKGELLKTERATELLPKLLCLQVLRLEGNTLGE----------------EAAKALASALRPQPSL--------KELCLS 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 625 LYETQED-AFVRQALCRFPELA-LQRVRfcRMDVAVlsycvrcCPAGQAlRLISCRLVAAQEKKKK---SLGKRlqaslg 699
Cdd:cd00116   60 LNETGRIpRGLQSLLQGLTKGCgLQELD--LSDNAL-------GPDGCG-VLESLLRSSSLQELKLnnnGLGDR------ 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 700 ggsssqgTTKQLPASLLhplfqamtDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEG 779
Cdd:cd00116  124 -------GLRLLAKGLK--------DLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEG 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 780 LAwPQCRVQTVRVQ---LPDpqRGLQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQ 856
Cdd:cd00116  189 LK-ANCNLEVLDLNnngLTD--EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDD 265
                        330
                 ....*....|....*.
gi 452085171 857 SLQELQAVKRAKPDLV 872
Cdd:cd00116  266 GAKDLAEVLAEKESLL 281
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
442-497 1.84e-06

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 45.63  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 452085171  442 LRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPgVLETEVTYQF 497
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
729-868 1.25e-05

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: 48.63  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 729 HLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLawpQCRVQTVRVQLPDPQRG-------L 801
Cdd:COG5238  293 TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL---QENTTLHSLDLSDNQIGdegaialA 369
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 802 QYLVGmlrqSPALTTLDLSGCQLPAPMVTYLCAVLQHQgcGLQTLSLASVELSEQSLQEL-QAVKRAK 868
Cdd:COG5238  370 KYLEG----NTTLRELNLGKNNIGKQGAEALIDALQTN--RLHTLILDGNLIGAEAQQRLeQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
725-880 3.25e-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: 43.88  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 725 DPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTEL--GLLHNRLSEAGLRMLSEGLAwPQCRVQTVRVQLPDPQRGLQ 802
Cdd:cd00116   20 PKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGC 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 803 YLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDG 880
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
197-350 1.25e-44

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: 158.24  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERPGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171  273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
501-636 1.28e-21

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: 91.20  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 452085171  571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
31-99 2.95e-21

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: 88.74  E-value: 2.95e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321   13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
35-782 2.63e-17

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 87.17  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171  35 KRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRAD-ARDVAAQLQERRLQRLGLGSGTLL 113
Cdd:COG5635   23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALsALLLVLLLLESLLLLLLLLLLLAE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 114 SVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEAMGPAEEPEPGRARRSDThTFNRLFRRDEEGR 193
Cdd:COG5635  103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIE-SLKRLELLEAKKK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 194 RpltVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVdFAFFMPCGELLERPgtrSLADLILDQCPDRGAPVPQM---LAQ 270
Cdd:COG5635  182 R---LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLAEEA---SLEDLLAEALEKRGGEPEDAlerLLR 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 271 PQRLLFILDGADELPalggpeaapctDPFEAASGARVLGGLLSKalLPTALLLVTTRAAA--PGRLQGRlcspQCAEVRG 348
Cdd:COG5635  255 NGRLLLLLDGLDEVP-----------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGydSSELEGF----EVLELAP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 349 FSDKDKKK-YFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRtsktttsVYLLFITSVL 427
Cdd:COG5635  318 LSDEQIEEfLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE-------LYEQFVELLL 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 428 SSAPVADGPRLQGDL------RNLCRLAREGVLGRRAQFAEKELEQL---ELRGSKVQTLFLSKKELPGVL---ETEVTY 495
Cdd:COG5635  391 ERWDEQRGLTIYRELsreelrELLSELALAMQENGRTEFAREELEEIlreYLGRRKDAEALLDELLLRTGLlveRGEGRY 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 496 QFIDQSFQEFLAALsYLLEDGGVPRTAAggvgtLLRGDAQPHSHLVLttRFLFGLLSaeRMRDIERHFGCMVSERVKQEA 575
Cdd:COG5635  471 SFAHRSFQEYLAAR-ALVEELDEELLEL-----LAEHLEDPRWREVL--LLLAGLLD--DVKQIKELIDALLARDDAAAL 540
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 576 LRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMD 655
Cdd:COG5635  541 ALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALAL 620
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 656 VAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLFQAMTDPLCHLSSLTL 735
Cdd:COG5635  621 LLALLLLLLLLLLAELLLLALLALVLLSLLLASRLLLITLLLLAAASAALLLLLLLLLAELLLALLALASLLLLLLLALA 700
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*..
gi 452085171 736 SHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAW 782
Cdd:COG5635  701 LALALLLLAVLLAAALDLLLLLVLLLALLLVLALALSLLLLALALLL 747
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
30-95 1.10e-16

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: 75.32  E-value: 1.10e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 452085171   30 SQEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAA 95
Cdd:pfam02758  10 SEEEFKKFKSLLEDEPEEGlRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
545-872 7.24e-14

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 73.54  E-value: 7.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 545 RFLFGLLSAERMRDIERHFGCMVSERVKQEALRWvqgqgqgcpgvapevtEGAKGLEDTEEPEEEEegeepnypLELLYC 624
Cdd:cd00116    4 SLKGELLKTERATELLPKLLCLQVLRLEGNTLGE----------------EAAKALASALRPQPSL--------KELCLS 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 625 LYETQED-AFVRQALCRFPELA-LQRVRfcRMDVAVlsycvrcCPAGQAlRLISCRLVAAQEKKKK---SLGKRlqaslg 699
Cdd:cd00116   60 LNETGRIpRGLQSLLQGLTKGCgLQELD--LSDNAL-------GPDGCG-VLESLLRSSSLQELKLnnnGLGDR------ 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 700 ggsssqgTTKQLPASLLhplfqamtDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEG 779
Cdd:cd00116  124 -------GLRLLAKGLK--------DLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEG 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 780 LAwPQCRVQTVRVQ---LPDpqRGLQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQ 856
Cdd:cd00116  189 LK-ANCNLEVLDLNnngLTD--EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDD 265
                        330
                 ....*....|....*.
gi 452085171 857 SLQELQAVKRAKPDLV 872
Cdd:cd00116  266 GAKDLAEVLAEKESLL 281
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
442-497 1.84e-06

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 45.63  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 452085171  442 LRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPgVLETEVTYQF 497
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
30-101 8.20e-06

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: 44.92  E-value: 8.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 452085171  30 SQEQLKRFRHKLRDVGPDGRS--IPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQERR 101
Cdd:cd08320    9 SKEELKKFKLLLKEESLEGGLkpIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARAEM 82
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
729-868 1.25e-05

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: 48.63  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 729 HLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLawpQCRVQTVRVQLPDPQRG-------L 801
Cdd:COG5238  293 TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL---QENTTLHSLDLSDNQIGdegaialA 369
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 802 QYLVGmlrqSPALTTLDLSGCQLPAPMVTYLCAVLQHQgcGLQTLSLASVELSEQSLQEL-QAVKRAK 868
Cdd:COG5238  370 KYLEG----NTTLRELNLGKNNIGKQGAEALIDALQTN--RLHTLILDGNLIGAEAQQRLeQLLERIK 431
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
709-863 1.16e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.69  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 709 KQLPASLLhplfqamtdPLCHLSSLTLSHCKLpdavcRDLSEALRAAPALTELGLLHNRLSEaglrmLSEGLAwpqcrvq 788
Cdd:COG4886  172 TDLPEELG---------NLTNLKELDLSNNQI-----TDLPEPLGNLTNLEELDLSGNQLTD-----LPEPLA------- 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 789 tvrvQLPdpqrGLQYL---------VGMLRQSPALTTLDLSGCQLpapmvTYLCAVLQHQgcGLQTLSLASVELSEQSLQ 859
Cdd:COG4886  226 ----NLT----NLETLdlsnnqltdLPELGNLTNLEELDLSNNQL-----TDLPPLANLT--NLKTLDLSNNQLTDLKLK 290

                 ....
gi 452085171 860 ELQA 863
Cdd:COG4886  291 ELEL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
730-861 1.18e-04

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: 45.55  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 730 LSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAwpqcRVQTVRV------QLPDpqRGLQY 803
Cdd:COG5238  266 VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQ----GNKTLHTlnlaynGIGA--QGAIA 339
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 804 LVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGcGLQTLSLASVELSEQSLQEL 861
Cdd:COG5238  340 LAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEAL 396
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
722-786 3.25e-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: 43.88  E-value: 3.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 452085171 722 AMTDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQCR 786
Cdd:cd00116  244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNE 308
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
725-880 3.25e-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: 43.88  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 725 DPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTEL--GLLHNRLSEAGLRMLSEGLAwPQCRVQTVRVQLPDPQRGLQ 802
Cdd:cd00116   20 PKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGC 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452085171 803 YLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDG 880
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
32-98 3.44e-04

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: 39.98  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 452085171  32 EQLKRFRHKLRDVGpdgrSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQ 98
Cdd:cd08305   11 EEFKMFKSLLASEL----KLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
729-861 4.89e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.38  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 729 HLSSLTLSHCKLpdavcRDLSEALRAAPALTELGLLHNRLSEaglrmLSEGLAwpqcrvqtvrvQLPdpqrGLQYLV--- 805
Cdd:COG4886  137 NLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNNQLTD-----LPEELG-----------NLT----NLKELDlsn 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 452085171 806 -------GMLRQSPALTTLDLSGCQ---LPAPMvtylcAVLQHqgcgLQTLSLASVELSE-------QSLQEL 861
Cdd:COG4886  192 nqitdlpEPLGNLTNLEELDLSGNQltdLPEPL-----ANLTN----LETLDLSNNQLTDlpelgnlTNLEEL 255
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
748-856 5.05e-04

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: 43.63  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 748 LSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQcRVQTVRV---QLPDPqrGLQYLVGMLRQSPALTTLDLSGCQL 824
Cdd:COG5238  228 LAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLsgnQIGAE--GAIALAKALQGNTTLTSLDLSVNRI 304
                         90       100       110
                 ....*....|....*....|....*....|..
gi 452085171 825 PAPMVTYLCAVLQHQGCgLQTLSLASVELSEQ 856
Cdd:COG5238  305 GDEGAIALAEGLQGNKT-LHTLNLAYNGIGAQ 335
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
727-861 6.32e-04

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: 43.24  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452085171 727 LCHLSSLT---LSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAwpqcRVQTVRV------QLPDP 797
Cdd:COG5238  232 LKGNKSLTtldLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ----GNTTLTSldlsvnRIGDE 307
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 452085171 798 qrGLQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQhQGCGLQTLSLASVELSEQSLQEL 861
Cdd:COG5238  308 --GAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQ-ENTTLHSLDLSDNQIGDEGAIAL 368
 
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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