|
Name |
Accession |
Description |
Interval |
E-value |
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
197-367 |
4.18e-48 |
|
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: 168.64 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729 2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729 80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151
|
170
....*....|....
gi 530384383 354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
730-950 |
8.50e-48 |
|
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: 176.52 E-value: 8.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 730 LTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 810 NSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530384383 890 EMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
|
|
| CARD_NOD1_CARD4 |
cd08324 |
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ... |
21-105 |
2.91e-45 |
|
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
:
Pssm-ID: 260035 Cd Length: 85 Bit Score: 157.25 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324 1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80
|
....*
gi 530384383 101 RPWLL 105
Cdd:cd08324 81 RPWLD 85
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
190-542 |
3.50e-21 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
:
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 99.88 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635 250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635 384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530384383 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635 457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
|
|
| NLRC4_HD2 super family |
cl39284 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
517-665 |
1.63e-11 |
|
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.
The actual alignment was detected with superfamily member pfam17776:
Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 62.31 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530384383 597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776 64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
197-367 |
4.18e-48 |
|
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: 168.64 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729 2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729 80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151
|
170
....*....|....
gi 530384383 354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
730-950 |
8.50e-48 |
|
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: 176.52 E-value: 8.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 730 LTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 810 NSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530384383 890 EMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
|
|
| CARD_NOD1_CARD4 |
cd08324 |
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ... |
21-105 |
2.91e-45 |
|
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260035 Cd Length: 85 Bit Score: 157.25 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324 1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80
|
....*
gi 530384383 101 RPWLL 105
Cdd:cd08324 81 RPWLD 85
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
676-941 |
6.01e-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: 106.67 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116 24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEG 828
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 829 AKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAE-MLKVNQTLKHLWLIQNQ 907
Cdd:cd00116 182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCND 261
|
250 260 270
....*....|....*....|....*....|....
gi 530384383 908 ITAKGTAQLADALQSNTGITEICLNGNLIKPEEA 941
Cdd:cd00116 262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
190-542 |
3.50e-21 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 99.88 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635 250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635 384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530384383 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635 457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
21-92 |
2.78e-16 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.
Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 74.52 E-value: 2.78e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530384383 21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619 2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE 73
|
|
| NLRC4_HD2 |
pfam17776 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
517-665 |
1.63e-11 |
|
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: 62.31 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530384383 597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776 64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
|
|
| NOD2_WH |
pfam17779 |
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
458-515 |
3.64e-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: 44.86 E-value: 3.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530384383 458 DTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELgPGGDQQSYEF 515
Cdd:pfam17779 1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
197-367 |
4.18e-48 |
|
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: 168.64 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729 2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSGNA--RSLADLLFSQWPEPAAPVSEVWAVILELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRKKVL-LRGFS 353
Cdd:pfam05729 80 ERLLLILDGLDELVSDLGQLDGPCP--------VLTLLSSLLRKKLLPGASLLLTVRPDAlrDLRRGLEEPRYLeVRGFS 151
|
170
....*....|....
gi 530384383 354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
730-950 |
8.50e-48 |
|
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: 176.52 E-value: 8.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 730 LTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVK 809
Cdd:COG5238 210 VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 810 NSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLA 889
Cdd:COG5238 290 GNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530384383 890 EMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTgITEICLNGNLIKPE-EAKVYEDEKRI 950
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEaQQRLEQLLERI 430
|
|
| CARD_NOD1_CARD4 |
cd08324 |
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ... |
21-105 |
2.91e-45 |
|
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260035 Cd Length: 85 Bit Score: 157.25 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324 1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80
|
....*
gi 530384383 101 RPWLL 105
Cdd:cd08324 81 RPWLD 85
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
676-941 |
6.01e-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: 106.67 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116 24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEG 828
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 829 AKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAE-MLKVNQTLKHLWLIQNQ 907
Cdd:cd00116 182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCND 261
|
250 260 270
....*....|....*....|....*....|....
gi 530384383 908 ITAKGTAQLADALQSNTGITEICLNGNLIKPEEA 941
Cdd:cd00116 262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
719-936 |
3.59e-24 |
|
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: 104.36 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 719 GVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYL--GLYNNQITDVGARYVTKILDECKGLTHLKLGKNKI 796
Cdd:cd00116 14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 797 TSEGGKYLALAVKNSkSISEVGMWGNQVGDEGAKAFAEALRNH-PSLTTLSLASNGISTEGGKSLARALQQNTSLEILWL 875
Cdd:cd00116 94 GPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALAKALRANRDLKELNL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530384383 876 TQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLI 936
Cdd:cd00116 173 ANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL 233
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
723-896 |
4.70e-23 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 101.28 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 723 LQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGK 802
Cdd:cd00116 132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 803 YLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRN-HPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELN 881
Cdd:cd00116 212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291
|
170
....*....|....*
gi 530384383 882 DEVAESLAEMLKVNQ 896
Cdd:cd00116 292 EEGAQLLAESLLEPG 306
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
190-542 |
3.50e-21 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 99.88 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 190 ILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFScfKESDrlcLQDLLFKHYCYPERDPEEVF 269
Cdd:COG5635 175 LLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLA--EEAS---LEDLLAEALEKRGGEPEDAL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 270 AFLLRFPHVALFtFDGLDELHSDLDLSRVpdsscpwepahpLVLLANLLSGklLKGASKLLTARTgIEVPRQFLR--KKV 347
Cdd:COG5635 250 ERLLRNGRLLLL-LDGLDEVPDEADRDEV------------LNQLRRFLER--YPKARVIITSRP-EGYDSSELEgfEVL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 348 LLRGFSPSHLRAYARRMFPERALQ-DRLLSQLEANPNLCSLCSVPLFCWIIfrCfqhfrAAFEGSPQLPDctmTLTDVFL 426
Cdd:COG5635 314 ELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPLLLTLL--A-----LLLRERGELPD---TRAELYE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 427 LVTEVHLNRMQpsslVQRNTRSPVETLHAGRDTLcsLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLG---FLRALpE 503
Cdd:COG5635 384 QFVELLLERWD----EQRGLTIYRELSREELREL--LSELALAMQENGRTEFAREELEEILREYLGRRKDaeaLLDEL-L 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530384383 504 LGPG----GDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLR 542
Cdd:COG5635 457 LRTGllveRGEGRYSFAHRSFQEYLAARALVEELDEELLELLA 499
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
728-920 |
2.22e-17 |
|
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: 84.33 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 728 SRLTVLRLSVNQITDGGVKVLSEELTKYKI-VTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLAL 806
Cdd:cd00116 108 SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 807 AVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARAL-QQNTSLEILWLTQNELNDEVA 885
Cdd:cd00116 188 GLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGA 267
|
170 180 190
....*....|....*....|....*....|....*
gi 530384383 886 ESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADAL 920
Cdd:cd00116 268 KDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
21-92 |
2.78e-16 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.
Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 74.52 E-value: 2.78e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530384383 21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619 2 KLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKE 73
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
727-936 |
2.47e-15 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 79.21 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGAryvtkILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886 135 LTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPE-----ELGNLTNLKELDLSNNQITD-----LPE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 807 AVKNSKSISEVGMWGNQVGDegakaFAEALRNHPSLTTLSLASNGISTeggkslARALQQNTSLEILWLTQNELNDevAE 886
Cdd:COG4886 200 PLGNLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTD--LP 266
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530384383 887 SLAEMlkvnQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLI 936
Cdd:COG4886 267 PLANL----TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
727-942 |
6.60e-15 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 78.05 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 727 FSRLTVLRLSVNqitdggvkvlsEELTKYKIVTYLGLYNNQITDVGARyvtkiLDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886 95 LTNLTELDLSGN-----------EELSNLTNLESLDLSGNQLTDLPEE-----LANLTNLKELDLSNNQLTD-----LPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 807 AVKNSKSISEVGMWGNQVGDegakaFAEALRNHPSLTTLSLASNGISteggkSLARALQQNTSLEILWLTQNELNDeVAE 886
Cdd:COG4886 154 PLGNLTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTD-LPE 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530384383 887 SLAEMlkvnQTLKHLWLIQNQITAkgtaqlADALQSNTGITEICLNGNLIK--PEEAK 942
Cdd:COG4886 223 PLANL----TNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTdlPPLAN 270
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
727-942 |
4.80e-13 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 72.27 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 727 FSRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDVGaryvtKILDECKGLTHLKLGKNKITSeggkyLAL 806
Cdd:COG4886 158 LTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITDLP-----EPLGNLTNLEELDLSGNQLTD-----LPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 807 AVKNSKSISEVGMWGNQVGDegakafAEALRNHPSLTTLSLASNGISTEGgkslarALQQNTSLEILWLTQNELNDEVAE 886
Cdd:COG4886 223 PLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTDLP------PLANLTNLKTLDLSNNQLTDLKLK 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530384383 887 SLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAK 942
Cdd:COG4886 291 ELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
|
|
| CARD |
cd01671 |
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
23-92 |
1.06e-11 |
|
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 61.38 E-value: 1.06e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 23 LKSNRELLVTHIrNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:cd01671 1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRE 69
|
|
| NLRC4_HD2 |
pfam17776 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
517-665 |
1.63e-11 |
|
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: 62.31 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 517 HLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMppagaaTTSCYPPFLpfqclqgsgpaREDLFKNKDHFQFTNLFLCGLL 596
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR------KRESLKSLL-----------DKALKSKNGHLDLFLRFLFGLL 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530384383 597 SKAKQKLLRHLVPAAALRRKRKalwahlfsSLRGYLKSLPRVQVESFNqvqamptFIWMLRCIYETQSQ 665
Cdd:pfam17776 64 NEENQRLLEGLLGCKLSSEIKQ--------ELLQWIKSLIQKELSSER-------FLNLFHCLYELQDE 117
|
|
| NOD2_WH |
pfam17779 |
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
458-515 |
3.64e-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: 44.86 E-value: 3.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530384383 458 DTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELgPGGDQQSYEF 515
Cdd:pfam17779 1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
|
|
| CARD_RIP2_CARD3 |
cd08786 |
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ... |
21-91 |
1.67e-04 |
|
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 176764 Cd Length: 87 Bit Score: 41.45 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530384383 21 QLLKSNRELLV---THIRNTQCLvDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQ 91
Cdd:cd08786 1 QWIASKREEIVsqmTEACLNQSL-DALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQKLK 73
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
727-911 |
2.82e-04 |
|
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.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 43.24 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 727 FSRLTVLRLSVNQITDggvkvlSEELTKYKIVTYLGLYNNQITdvgaryvtKI--LDECKGLTHLKLGKNKITS-EGgky 803
Cdd:cd21340 1 LKRITHLYLNDKNITK------IDNLSLCKNLKVLYLYDNKIT--------KIenLEFLTNLTHLYLQNNQIEKiEN--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 804 LALAVKNSK------SISEV-GMWG----------NQVGDEGAK-AF----AEALRNhpSLTTLSLASNGISTeggkslA 861
Cdd:cd21340 64 LENLVNLKKlylggnRISVVeGLENltnleelhieNQRLPPGEKlTFdprsLAALSN--SLRVLNISGNNIDS------L 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530384383 862 RALQQNTSLEILWLTQNELNDevAESLAEMLKVNQTLKHLWLIQNQITAK 911
Cdd:cd21340 136 EPLAPLRNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVCKK 183
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
727-910 |
3.65e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 44.15 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 727 FSRLTVLRLSVNQITDggVKVLSEeLTKykiVTYLGLYNNQITDVGAryvtkiLDECKGLTHLKLGKNKITSEGGKYLAL 806
Cdd:COG4886 227 LTNLETLDLSNNQLTD--LPELGN-LTN---LEELDLSNNQLTDLPP------LANLTNLKTLDLSNNQLTDLKLKELEL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530384383 807 AVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAE 886
Cdd:COG4886 295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGL 374
|
170 180
....*....|....*....|....
gi 530384383 887 SLAEMLKVNQTLKHLWLIQNQITA 910
Cdd:COG4886 375 LEATLLTLALLLLTLLLLLLTTTA 398
|
|
| CARD_NOD2_2_CARD15 |
cd08788 |
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ... |
23-95 |
9.90e-04 |
|
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260056 Cd Length: 81 Bit Score: 39.00 E-value: 9.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530384383 23 LKSNRELLVTHIR-NTQCLVDNLLKNDYFSAEDA-EIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLAD 95
Cdd:cd08788 1 LQTQRPALVRRLRdHVDGALELLLTRGFFSQYDCdEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPE 75
|
|
| CARD_BIRC2_BIRC3 |
cd08329 |
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
20-97 |
4.40e-03 |
|
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260038 Cd Length: 94 Bit Score: 37.42 E-value: 4.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530384383 20 IQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQlADAY 97
Cdd:cd08329 8 LSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKE-IDVV 84
|
|
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