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Conserved domains on  [gi|5174617|ref|NP_006083|]
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nucleotide-binding oligomerization domain-containing protein 1 isoform 1 [Homo sapiens]

Protein Classification

CARD_NOD1_CARD4 and NACHT domain-containing protein (domain architecture ID 11579492)

protein containing domains CARD_NOD1_CARD4, COG5635, NACHT, and LRR_RI

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 ...
197-367 2.25e-47

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: 310381  Cd Length: 166  Bit Score: 168.25  E-value: 2.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKIALLWAQGKLPQGFDFVFFLPCRELSRSGNA--LSLADLLFSQWPEPAAPVSEVFAVILELP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRK-KVLLRGFS 353
Cdd:pfam05729  80 DRLLLILDGLDELVSDLGQLDGPCP--------VRTLLSSLLRKKLLPGASLLLTSRPDAlrDLRRGLEEPrYLEVRGFS 151
                         170
                  ....*....|....
gi 5174617    354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 EDDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
21-105 1.83e-44

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: 1.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617   21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80

                ....*
gi 5174617  101 RPWLL 105
Cdd:cd08324  81 RPWLD 85
LRR_RI super family cl26161
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
676-941 1.35e-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).


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 330982  Cd Length: 319  Bit Score: 106.67  E-value: 1.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116  24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEG 828
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  829 AKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAE-MLKVNQTLKHLWLIQNQ 907
Cdd:cd00116 182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCND 261
                       250       260       270
                ....*....|....*....|....*....|....
gi 5174617  908 ITAKGTAQLADALQSNTGITEICLNGNLIKPEEA 941
Cdd:cd00116 262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
COG5635 super family cl26020
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
170-542 4.04e-03

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


The actual alignment was detected with superfamily member COG5635:

Pssm-ID: 227922  Cd Length: 824  Bit Score: 40.93  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  170 SNESLGSLNSLACLLDHTTGILN--EQGETIFILGDAGVGKSMLLQRLQSLWATGRL-DAGVKFFFHFRCRMFSCfKESD 246
Cdd:COG5635 195 FDEEFLLELTQSADDQDALPGLEalEKYAKLLILGAPGSGKTTFLQRLALWLAQRTLePEDVPIFLLLNAFALAR-KFEK 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  247 RLCLQDLL--FKHYCYPERDPEEVFAFLLRFPHVALFtFDGLDEL---HSDLDLSRVPDSScPWEPaHPLVLLA------ 315
Cdd:COG5635 274 QLSLIDYLaeELFSQGIAKQLIEAHQELLKTGKLLLL-LDGLDELepkNQRALIREINKFL-QEYP-DAQVLLTcrpdty 350
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  316 -NLLSGKLLKGASKLltartGIEVPRQFLRKKVLLRgfsPSHLRAYARRmFPERALQDRLlsQLEANPNLCSLCSVPLFc 394
Cdd:COG5635 351 kEEFKGFAVFEIYKF-----LDLQINQFILYQWLDA---FIEDWFGDSR-LLAKKLLERL--KLPENRRIKELALTPLL- 418
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  395 wiIFRCFQHFRaafegspQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETL-HAGRDTLCSLGQVAHRGMEK 473
Cdd:COG5635 419 --LALECLIWQ-------AQGDLPESRAELYEQAVDALLGREDETRGIKWSKTYAKLTTdQQDKWLLQLLAALLFEKLDE 489
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  474 SLFVFTQEEVQASGLQER--DMQLGFLRALPELGP------------GGDQqsYEFFHLTLQAFFTAFFLVLDDRVGTQE 539
Cdd:COG5635 490 EFTEFLLKDDIVDYLLNQaeDEDDLIALALALEALlkllqhgllverAKIV--YAFAHATFQEYFAAKKIVASSPSQKLE 567

                ...
gi 5174617  540 LLR 542
Cdd:COG5635 568 SLI 570
 
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 2.25e-47

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: 310381  Cd Length: 166  Bit Score: 168.25  E-value: 2.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKIALLWAQGKLPQGFDFVFFLPCRELSRSGNA--LSLADLLFSQWPEPAAPVSEVFAVILELP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRK-KVLLRGFS 353
Cdd:pfam05729  80 DRLLLILDGLDELVSDLGQLDGPCP--------VRTLLSSLLRKKLLPGASLLLTSRPDAlrDLRRGLEEPrYLEVRGFS 151
                         170
                  ....*....|....
gi 5174617    354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 EDDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
21-105 1.83e-44

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: 1.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617   21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80

                ....*
gi 5174617  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 1.35e-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  Cd Length: 319  Bit Score: 106.67  E-value: 1.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116  24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEG 828
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  829 AKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAE-MLKVNQTLKHLWLIQNQ 907
Cdd:cd00116 182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCND 261
                       250       260       270
                ....*....|....*....|....*....|....
gi 5174617  908 ITAKGTAQLADALQSNTGITEICLNGNLIKPEEA 941
Cdd:cd00116 262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
21-92 3.14e-15

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 306972  Cd Length: 85  Bit Score: 73.75  E-value: 3.14e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174617     21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619   2 ELLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANTTRLDKARKLLDLVLKKGPEACQIFLEALKE 73
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal ...
741-917 1.49e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal transduction mechanisms, RNA processing and modification];


Pssm-ID: 227563  Cd Length: 388  Bit Score: 51.47  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  741 TDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGL-------THLKLGKNKITsEGGKYLALAVKNSKS 813
Cdd:COG5238  15 TKEDVKGVVEELEMMDELVEVDLSGNTIGTEAMEELCNVIANVRNLrvvnfsdAFTGRDKDELY-SNLVMLLKALLKCPR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  814 ISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQ---------NTSLEILWLTQNELNDEV 884
Cdd:COG5238  94 LQKVDLSDNAFGSEFPEELGDLISSSTDLVHLKLNNNGLGPIAGGRIGKALFHlaynkkaadKPKLEVVICGRNRLENGS 173
                       170       180       190
                ....*....|....*....|....*....|...
gi 5174617  885 AESLAEMLKVNQTLKHLWLIQNQITAKGTAQLA 917
Cdd:COG5238 174 KELSAALLESHENLKEVKIQQNGIRPEGVTMLA 206
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
194-291 3.07e-03

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


Pssm-ID: 214640  Cd Length: 148  Bit Score: 38.89  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617     194 QGETIFILGDAGVGKSMLLQRLQslwatGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLL 273
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA-----RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR 75
                           90
                   ....*....|....*...
gi 5174617     274 RFPHVALFtfdgLDELHS 291
Cdd:smart00382  76 KLKPDVLI----LDEITS 89
COG5635 COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
170-542 4.04e-03

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


Pssm-ID: 227922  Cd Length: 824  Bit Score: 40.93  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  170 SNESLGSLNSLACLLDHTTGILN--EQGETIFILGDAGVGKSMLLQRLQSLWATGRL-DAGVKFFFHFRCRMFSCfKESD 246
Cdd:COG5635 195 FDEEFLLELTQSADDQDALPGLEalEKYAKLLILGAPGSGKTTFLQRLALWLAQRTLePEDVPIFLLLNAFALAR-KFEK 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  247 RLCLQDLL--FKHYCYPERDPEEVFAFLLRFPHVALFtFDGLDEL---HSDLDLSRVPDSScPWEPaHPLVLLA------ 315
Cdd:COG5635 274 QLSLIDYLaeELFSQGIAKQLIEAHQELLKTGKLLLL-LDGLDELepkNQRALIREINKFL-QEYP-DAQVLLTcrpdty 350
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  316 -NLLSGKLLKGASKLltartGIEVPRQFLRKKVLLRgfsPSHLRAYARRmFPERALQDRLlsQLEANPNLCSLCSVPLFc 394
Cdd:COG5635 351 kEEFKGFAVFEIYKF-----LDLQINQFILYQWLDA---FIEDWFGDSR-LLAKKLLERL--KLPENRRIKELALTPLL- 418
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  395 wiIFRCFQHFRaafegspQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETL-HAGRDTLCSLGQVAHRGMEK 473
Cdd:COG5635 419 --LALECLIWQ-------AQGDLPESRAELYEQAVDALLGREDETRGIKWSKTYAKLTTdQQDKWLLQLLAALLFEKLDE 489
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  474 SLFVFTQEEVQASGLQER--DMQLGFLRALPELGP------------GGDQqsYEFFHLTLQAFFTAFFLVLDDRVGTQE 539
Cdd:COG5635 490 EFTEFLLKDDIVDYLLNQaeDEDDLIALALALEALlkllqhgllverAKIV--YAFAHATFQEYFAAKKIVASSPSQKLE 567

                ...
gi 5174617  540 LLR 542
Cdd:COG5635 568 SLI 570
 
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 2.25e-47

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: 310381  Cd Length: 166  Bit Score: 168.25  E-value: 2.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    197 TIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESdrLCLQDLLFKHYCYPERDPEEVFAFLLRFP 276
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKIALLWAQGKLPQGFDFVFFLPCRELSRSGNA--LSLADLLFSQWPEPAAPVSEVFAVILELP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617    277 HVALFTFDGLDELHSDLDLSRVPDSscpwepahPLVLLANLLSGKLLKGASKLLTARTGI--EVPRQFLRK-KVLLRGFS 353
Cdd:pfam05729  80 DRLLLILDGLDELVSDLGQLDGPCP--------VRTLLSSLLRKKLLPGASLLLTSRPDAlrDLRRGLEEPrYLEVRGFS 151
                         170
                  ....*....|....
gi 5174617    354 PSHLRAYARRMFPE 367
Cdd:pfam05729 152 EDDRKQYVRKYFSD 165
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
21-105 1.83e-44

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: 1.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617   21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDL 100
Cdd:cd08324   1 QLLKSHRELLVSHIRNTQCLLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQKVADAYIDL 80

                ....*
gi 5174617  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 1.35e-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  Cd Length: 319  Bit Score: 106.67  E-value: 1.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  676 CANYLKLTYCNACSADCSALSFVLHHFP--KRLALDLDNNNLNDYGVRELqPCF----SRLTVLRLSVNQITDGGVKVLs 749
Cdd:cd00116  24 CLQVLRLEGNTLGEEAAKALASALRPQPslKELCLSLNETGRIPRGLQSL-LQGltkgCGLQELDLSDNALGPDGCGVL- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  750 EELTKYKIVTYLGLYNNQITDVGARYVTKILDECK-GLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEG 828
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  829 AKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAE-MLKVNQTLKHLWLIQNQ 907
Cdd:cd00116 182 IRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCND 261
                       250       260       270
                ....*....|....*....|....*....|....
gi 5174617  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 7.48e-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  Cd Length: 319  Bit Score: 104.36  E-value: 7.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  719 GVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYL--GLYNNQITDVGARYVTKILDECKGLTHLKLGKNKI 796
Cdd:cd00116  14 RATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  797 TSEGGKYLALAVKNSkSISEVGMWGNQVGDEGAKAFAEALRNH-PSLTTLSLASNGISTEGGKSLARALQQNTSLEILWL 875
Cdd:cd00116  94 GPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALAKALRANRDLKELNL 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5174617  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 8.74e-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  Cd Length: 319  Bit Score: 101.28  E-value: 8.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  723 LQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGK 802
Cdd:cd00116 132 LKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  803 YLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRN-HPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELN 881
Cdd:cd00116 212 ALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291
                       170
                ....*....|....*
gi 5174617  882 DEVAESLAEMLKVNQ 896
Cdd:cd00116 292 EEGAQLLAESLLEPG 306
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
728-920 2.16e-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  Cd Length: 319  Bit Score: 84.33  E-value: 2.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  728 SRLTVLRLSVNQITDGGVKVLSEELTKYKI-VTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLAL 806
Cdd:cd00116 108 SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAE 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  807 AVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARAL-QQNTSLEILWLTQNELNDEVA 885
Cdd:cd00116 188 GLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGA 267
                       170       180       190
                ....*....|....*....|....*....|....*
gi 5174617  886 ESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADAL 920
Cdd:cd00116 268 KDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
21-92 3.14e-15

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 306972  Cd Length: 85  Bit Score: 73.75  E-value: 3.14e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5174617     21 QLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:pfam00619   2 ELLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANTTRLDKARKLLDLVLKKGPEACQIFLEALKE 73
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
23-92 5.47e-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  Cd Length: 79  Bit Score: 61.38  E-value: 5.47e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617   23 LKSNRELLVTHIrNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQ 92
Cdd:cd01671   1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRE 69
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal ...
741-917 1.49e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal transduction mechanisms, RNA processing and modification];


Pssm-ID: 227563  Cd Length: 388  Bit Score: 51.47  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  741 TDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGL-------THLKLGKNKITsEGGKYLALAVKNSKS 813
Cdd:COG5238  15 TKEDVKGVVEELEMMDELVEVDLSGNTIGTEAMEELCNVIANVRNLrvvnfsdAFTGRDKDELY-SNLVMLLKALLKCPR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  814 ISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQ---------NTSLEILWLTQNELNDEV 884
Cdd:COG5238  94 LQKVDLSDNAFGSEFPEELGDLISSSTDLVHLKLNNNGLGPIAGGRIGKALFHlaynkkaadKPKLEVVICGRNRLENGS 173
                       170       180       190
                ....*....|....*....|....*....|...
gi 5174617  885 AESLAEMLKVNQTLKHLWLIQNQITAKGTAQLA 917
Cdd:COG5238 174 KELSAALLESHENLKEVKIQQNGIRPEGVTMLA 206
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal ...
812-921 3.77e-05

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal transduction mechanisms, RNA processing and modification];


Pssm-ID: 227563  Cd Length: 388  Bit Score: 46.84  E-value: 3.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  812 KSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGIS------TEGGKSLARALQQNTSLEILWLTQNELNDEVA 885
Cdd:COG5238  30 DELVEVDLSGNTIGTEAMEELCNVIANVRNLRVVNFSDAFTGrdkdelYSNLVMLLKALLKCPRLQKVDLSDNAFGSEFP 109
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5174617  886 ESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQ 921
Cdd:COG5238 110 EELGDLISSSTDLVHLKLNNNGLGPIAGGRIGKALF 145
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
21-91 3.29e-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: 3.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174617   21 QLLKSNRELLV---THIRNTQCLvDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQ 91
Cdd:cd08786   1 QWIASKREEIVsqmTEACLNQSL-DALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQKLK 73
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
728-939 4.29e-04

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


Pssm-ID: 227223  Cd Length: 394  Bit Score: 43.42  E-value: 4.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  728 SRLTVLRLSVNQITDggvkvLSEELTKYKIVTYLGLYNNQITDvgaryVTKILDECKGLTHLKLGKNKITSeggkyLALA 807
Cdd:COG4886 140 SNLKELDLSDNKIES-----LPSPLRNLPNLKNLDLSFNDLSD-----LPKLLSNLSNLNNLDLSGNKISD-----LPPE 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  808 VKNSKSISEVGMWGNQvgdegAKAFAEALRNHPSLTTLSLASNGIsteggKSLARALQQNTSLEILWLTQNELNDevaes 887
Cdd:COG4886 205 IELLSALEELDLSNNS-----IIELLSSLSNLKNLSGLELSNNKL-----EDLPESIGNLSNLETLDLSNNQISS----- 269
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5174617  888 lAEMLKVNQTLKHLWLIQNQIT----AKGTAQLADALQSNTGITEICLNGNLIKPE 939
Cdd:COG4886 270 -ISSLGSLTNLRELDLSGNSLSnalpLIALLLLLLELLLNLLLTLKALELKLNSIL 324
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal ...
729-919 8.01e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal transduction mechanisms, RNA processing and modification];


Pssm-ID: 227563  Cd Length: 388  Bit Score: 42.61  E-value: 8.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  729 RLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDEckglthlkLGKNKitseggkylalAV 808
Cdd:COG5238  93 RLQKVDLSDNAFGSEFPEELGDLISSSTDLVHLKLNNNGLGPIAGGRIGKALFH--------LAYNK-----------KA 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  809 KNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLA-RALQQNTSLEILWLTQNELNDEVAES 887
Cdd:COG5238 154 ADKPKLEVVICGRNRLENGSKELSAALLESHENLKEVKIQQNGIRPEGVTMLAfLGLFYSHSLEVLDLQDNTFTLEGSRY 233
                       170       180       190
                ....*....|....*....|....*....|..
gi 5174617  888 LAEMLKVNQTLKHLWLIQNQITAKGTAQLADA 919
Cdd:COG5238 234 LADALCEWNLLRELRLNDCLLSNEGVKSVLRR 265
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal ...
776-939 1.59e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Signal transduction mechanisms, RNA processing and modification];


Pssm-ID: 227563  Cd Length: 388  Bit Score: 41.84  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  776 VTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGM---WGNQVGDE---GAKAFAEALRNHPSLTTLSLAS 849
Cdd:COG5238  22 VVEELEMMDELVEVDLSGNTIGTEAMEELCNVIANVRNLRVVNFsdaFTGRDKDElysNLVMLLKALLKCPRLQKVDLSD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  850 NGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKH------LWLI---QNQITAKGTAQLADAL 920
Cdd:COG5238 102 NAFGSEFPEELGDLISSSTDLVHLKLNNNGLGPIAGGRIGKALFHLAYNKKaadkpkLEVVicgRNRLENGSKELSAALL 181
                       170
                ....*....|....*....
gi 5174617  921 QSNTGITEICLNGNLIKPE 939
Cdd:COG5238 182 ESHENLKEVKIQQNGIRPE 200
CARD_NOD2_2_CARD15 cd08788
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ...
23-95 1.87e-03

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: 1.87e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5174617   23 LKSNRELLVTHIR-NTQCLVDNLLKNDYFSAEDA-EIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLAD 95
Cdd:cd08788   1 LQTQRPALVRRLRdHVDGALELLLTRGFFSQYDCdEIRLPIFTPSQQARRLLDLVKAKGEGAAKFLLQYVQQLPE 75
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
194-291 3.07e-03

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


Pssm-ID: 214640  Cd Length: 148  Bit Score: 38.89  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617     194 QGETIFILGDAGVGKSMLLQRLQslwatGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLL 273
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA-----RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR 75
                           90
                   ....*....|....*...
gi 5174617     274 RFPHVALFtfdgLDELHS 291
Cdd:smart00382  76 KLKPDVLI----LDEITS 89
COG5635 COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
170-542 4.04e-03

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


Pssm-ID: 227922  Cd Length: 824  Bit Score: 40.93  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  170 SNESLGSLNSLACLLDHTTGILN--EQGETIFILGDAGVGKSMLLQRLQSLWATGRL-DAGVKFFFHFRCRMFSCfKESD 246
Cdd:COG5635 195 FDEEFLLELTQSADDQDALPGLEalEKYAKLLILGAPGSGKTTFLQRLALWLAQRTLePEDVPIFLLLNAFALAR-KFEK 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  247 RLCLQDLL--FKHYCYPERDPEEVFAFLLRFPHVALFtFDGLDEL---HSDLDLSRVPDSScPWEPaHPLVLLA------ 315
Cdd:COG5635 274 QLSLIDYLaeELFSQGIAKQLIEAHQELLKTGKLLLL-LDGLDELepkNQRALIREINKFL-QEYP-DAQVLLTcrpdty 350
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  316 -NLLSGKLLKGASKLltartGIEVPRQFLRKKVLLRgfsPSHLRAYARRmFPERALQDRLlsQLEANPNLCSLCSVPLFc 394
Cdd:COG5635 351 kEEFKGFAVFEIYKF-----LDLQINQFILYQWLDA---FIEDWFGDSR-LLAKKLLERL--KLPENRRIKELALTPLL- 418
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  395 wiIFRCFQHFRaafegspQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETL-HAGRDTLCSLGQVAHRGMEK 473
Cdd:COG5635 419 --LALECLIWQ-------AQGDLPESRAELYEQAVDALLGREDETRGIKWSKTYAKLTTdQQDKWLLQLLAALLFEKLDE 489
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  474 SLFVFTQEEVQASGLQER--DMQLGFLRALPELGP------------GGDQqsYEFFHLTLQAFFTAFFLVLDDRVGTQE 539
Cdd:COG5635 490 EFTEFLLKDDIVDYLLNQaeDEDDLIALALALEALlkllqhgllverAKIV--YAFAHATFQEYFAAKKIVASSPSQKLE 567

                ...
gi 5174617  540 LLR 542
Cdd:COG5635 568 SLI 570
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-937 4.89e-03

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


Pssm-ID: 227223  Cd Length: 394  Bit Score: 40.34  E-value: 4.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  730 LTVLRLSVNQItdggvKVLSEELTKYKIVTYLGLYNNQITDVgaryVTKILDECKGLTHLKLGKNKITSeggkyLALAVK 809
Cdd:COG4886  95 LPSLDLNLNRL-----RSNISELLELTNLTSLDLDNNNITDI----PPLIGLLKSNLKELDLSDNKIES-----LPSPLR 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174617  810 NSKSISEVGMWGNQVgdegaKAFAEALRNHPSLTTLSLASNGISteggkSLARALQQNTSLEILWLTQNELndevaESLA 889
Cdd:COG4886 161 NLPNLKNLDLSFNDL-----SDLPKLLSNLSNLNNLDLSGNKIS-----DLPPEIELLSALEELDLSNNSI-----IELL 225
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5174617  890 EMLKVNQTLKHLWLIQNQITakgtaQLADALQSNTGITEICLNGNLIK 937
Cdd:COG4886 226 SSLSNLKNLSGLELSNNKLE-----DLPESIGNLSNLETLDLSNNQIS 268
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
20-97 5.70e-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: 5.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5174617   20 IQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQlADAY 97
Cdd:cd08329   8 LSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKE-IDVV 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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