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Conserved domains on  [gi|123796288|sp|Q2LKW6|]
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RecName: Full=NACHT, LRR and PYD domains-containing protein 1b allele 1; Contains: RecName: Full=NACHT, LRR and PYD domains-containing protein 1b, C-terminus; Short=Nlrp1b1-CT; Contains: RecName: Full=NACHT, LRR and PYD domains-containing protein 1b, N-terminus; Short=Nlrp1b1-NT

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 871-1123 1.19e-140

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


:

Pssm-ID: 463919  Cd Length: 252  Bit Score: 426.30  E-value: 1.19e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   871 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 950
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   951 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 1030
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  1031 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1109
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 123796288  1110 HMKLIWEALLKPGD 1123
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 126-295 2.81e-41

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: 149.38  E-value: 2.81e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   126 QLVIIEGAAGIGKSTLARLVKRAWKEGQLYRDhFQHVFFFSCRELA-QCKKLSLAELIAQGQEVPTAPINQ----ILSHP 200
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   201 EKLLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPEAFFLLTTRTTALQKFIPSLPMPCQVEVLGFS 280
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 123796288   281 GIERENYFYKYFANQ 295
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1143-1223 3.85e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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: 260039  Cd Length: 81  Bit Score: 142.74  E-value: 3.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288 1143 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1222
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 123796288 1223 L 1223
Cdd:cd08330    81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 421-533 2.85e-28

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: 110.46  E-value: 2.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   421 HLCLQEFFAAISCILEDSEERH-------GNMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLGKEGVKGMEKLFSCSLH 493
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 123796288   494 GKTNLKLLWHILVKSQPHQPP--CLGLLHCLYENQDMELLTH 533
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSSerFLNLFHCLYELQDESFVKE 122
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 622-720 1.38e-12

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


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 70.08  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  622 LKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGDDGVR 701
Cdd:cd00116   217 LASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                          90
                  ....*....|....*....
gi 123796288  702 MLCEGLRNPVCNLSILWLD 720
Cdd:cd00116   297 LLAESLLEPGNELESLWVK 315
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 365-419 2.78e-08

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: 51.41  E-value: 2.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 123796288   365 QVKALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVATFLKTGVLQKQASSLS-YSF 419
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 871-1123 1.19e-140

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 426.30  E-value: 1.19e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   871 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 950
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   951 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 1030
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  1031 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1109
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 123796288  1110 HMKLIWEALLKPGD 1123
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 126-295 2.81e-41

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: 149.38  E-value: 2.81e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   126 QLVIIEGAAGIGKSTLARLVKRAWKEGQLYRDhFQHVFFFSCRELA-QCKKLSLAELIAQGQEVPTAPINQ----ILSHP 200
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   201 EKLLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPEAFFLLTTRTTALQKFIPSLPMPCQVEVLGFS 280
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 123796288   281 GIERENYFYKYFANQ 295
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1143-1223 3.85e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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: 260039  Cd Length: 81  Bit Score: 142.74  E-value: 3.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288 1143 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1222
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 123796288 1223 L 1223
Cdd:cd08330    81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 421-533 2.85e-28

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: 110.46  E-value: 2.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   421 HLCLQEFFAAISCILEDSEERH-------GNMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLGKEGVKGMEKLFSCSLH 493
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 123796288   494 GKTNLKLLWHILVKSQPHQPP--CLGLLHCLYENQDMELLTH 533
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSSerFLNLFHCLYELQDESFVKE 122
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
122-477 1.29e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 108.35  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  122 QKEPQLVIIEGAAGIGKSTLAR-LVKRAWKEGQLYRDHFqhVFFFSCRELAqcKKLSLAELIAQG-QEVPTAPINQI--L 197
Cdd:COG5635   177 EAKKKRLLILGEPGSGKTTLLRyLALELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEAlEKRGGEPEDALerL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  198 SHPEKLLFILDGIDEpawvLADQNpelclhwsQRQPVHTLLGSLLGKsiLPEAFFLLTTRTTALQ-KFIPSLPmpcQVEV 276
Cdd:COG5635   253 LRNGRLLLLLDGLDE----VPDEA--------DRDEVLNQLRRFLER--YPKARVIITSRPEGYDsSELEGFE---VLEL 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  277 LGFSGIERENYFYKYFANQRHAITAFM-MVESNPVLLTLCEVPWVCWLVCTclkkQMEQGRVLslkSQTTTALCLKYLS- 354
Cdd:COG5635   316 APLSDEQIEEFLKKWFEATERKAERLLeALEENPELRELARNPLLLTLLAL----LLRERGEL---PDTRAELYEQFVEl 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  355 -LTIPDKHRRTQV----------KALCSLAAEGIWKRRTLFSESDL-------CKQGLDEDAVATFL--KTGVLQKQASS 414
Cdd:COG5635   389 lLERWDEQRGLTIyrelsreelrELLSELALAMQENGRTEFAREELeeilreyLGRRKDAEALLDELllRTGLLVERGEG 468

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123796288  415 lSYSFAHLCLQEFFAAiSCILEDSEErhgnmemdRIVETLVERYGRQNLFEapTVRFLFGLLG 477
Cdd:COG5635   469 -RYSFAHRSFQEYLAA-RALVEELDE--------ELLELLAEHLEDPRWRE--VLLLLAGLLD 519
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1142-1222 1.81e-21

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: 89.54  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  1142 LHFMDQHREQLVARVTSVDPLLDKLHG-LVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1220
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 123796288  1221 DL 1222
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 622-720 1.38e-12

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: 70.08  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  622 LKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGDDGVR 701
Cdd:cd00116   217 LASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                          90
                  ....*....|....*....
gi 123796288  702 MLCEGLRNPVCNLSILWLD 720
Cdd:cd00116   297 LLAESLLEPGNELESLWVK 315
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 365-419 2.78e-08

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: 51.41  E-value: 2.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 123796288   365 QVKALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVATFLKTGVLQKQASSLS-YSF 419
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 608-723 4.99e-06

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: 50.56  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  608 TPITNASWEILFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYpGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTE 687
Cdd:COG5238   218 NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTS 296

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 123796288  688 LYLQLNDLGDDGVRMLCEGLRNpvcNLSILWLDLSS 723
Cdd:COG5238   297 LDLSVNRIGDEGAIALAEGLQG---NKTLHTLNLAY 329
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
682-708 5.85e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 41.24  E-value: 5.85e-05
                            10        20
                    ....*....|....*....|....*..
gi 123796288    682 HSSLTELYLQLNDLGDDGVRMLCEGLR 708
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 871-1123 1.19e-140

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 426.30  E-value: 1.19e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   871 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 950
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   951 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 1030
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  1031 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1109
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 123796288  1110 HMKLIWEALLKPGD 1123
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 126-295 2.81e-41

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: 149.38  E-value: 2.81e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   126 QLVIIEGAAGIGKSTLARLVKRAWKEGQLYRDhFQHVFFFSCRELA-QCKKLSLAELIAQGQEVPTAPINQ----ILSHP 200
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   201 EKLLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPEAFFLLTTRTTALQKFIPSLPMPCQVEVLGFS 280
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 123796288   281 GIERENYFYKYFANQ 295
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1143-1223 3.85e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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: 260039  Cd Length: 81  Bit Score: 142.74  E-value: 3.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288 1143 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1222
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 123796288 1223 L 1223
Cdd:cd08330    81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 421-533 2.85e-28

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: 110.46  E-value: 2.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288   421 HLCLQEFFAAISCILEDSEERH-------GNMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLGKEGVKGMEKLFSCSLH 493
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 123796288   494 GKTNLKLLWHILVKSQPHQPP--CLGLLHCLYENQDMELLTH 533
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSSerFLNLFHCLYELQDESFVKE 122
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
122-477 1.29e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 108.35  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  122 QKEPQLVIIEGAAGIGKSTLAR-LVKRAWKEGQLYRDHFqhVFFFSCRELAqcKKLSLAELIAQG-QEVPTAPINQI--L 197
Cdd:COG5635   177 EAKKKRLLILGEPGSGKTTLLRyLALELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEAlEKRGGEPEDALerL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  198 SHPEKLLFILDGIDEpawvLADQNpelclhwsQRQPVHTLLGSLLGKsiLPEAFFLLTTRTTALQ-KFIPSLPmpcQVEV 276
Cdd:COG5635   253 LRNGRLLLLLDGLDE----VPDEA--------DRDEVLNQLRRFLER--YPKARVIITSRPEGYDsSELEGFE---VLEL 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  277 LGFSGIERENYFYKYFANQRHAITAFM-MVESNPVLLTLCEVPWVCWLVCTclkkQMEQGRVLslkSQTTTALCLKYLS- 354
Cdd:COG5635   316 APLSDEQIEEFLKKWFEATERKAERLLeALEENPELRELARNPLLLTLLAL----LLRERGEL---PDTRAELYEQFVEl 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  355 -LTIPDKHRRTQV----------KALCSLAAEGIWKRRTLFSESDL-------CKQGLDEDAVATFL--KTGVLQKQASS 414
Cdd:COG5635   389 lLERWDEQRGLTIyrelsreelrELLSELALAMQENGRTEFAREELeeilreyLGRRKDAEALLDELllRTGLLVERGEG 468

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123796288  415 lSYSFAHLCLQEFFAAiSCILEDSEErhgnmemdRIVETLVERYGRQNLFEapTVRFLFGLLG 477
Cdd:COG5635   469 -RYSFAHRSFQEYLAA-RALVEELDE--------ELLELLAEHLEDPRWRE--VLLLLAGLLD 519
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1142-1222 1.81e-21

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: 89.54  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  1142 LHFMDQHREQLVARVTSVDPLLDKLHG-LVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1220
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 123796288  1221 DL 1222
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 622-720 1.38e-12

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: 70.08  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  622 LKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGDDGVR 701
Cdd:cd00116   217 LASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                          90
                  ....*....|....*....
gi 123796288  702 MLCEGLRNPVCNLSILWLD 720
Cdd:cd00116   297 LLAESLLEPGNELESLWVK 315
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 618-739 3.62e-12

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: 68.92  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  618 LFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGD 697
Cdd:cd00116   100 VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGD 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 123796288  698 DGVRMLCEGLRNpVCNLSILWLDLSSLS-------AQVITELRTLEEKN 739
Cdd:cd00116   180 AGIRALAEGLKA-NCNLEVLDLNNNGLTdegasalAETLASLKSLEVLN 227
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 610-738 8.75e-12

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: 67.77  E-value: 8.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  610 ITNASWEILFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYpGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELY 689
Cdd:cd00116   149 LEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 123796288  690 LQLNDLGDDGVRMLCEGLRNPVCNLSILWLDLSSLSAQ-VITELRTLEEK 738
Cdd:cd00116   228 LGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDgAKDLAEVLAEK 277
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 1147-1223 3.03e-09

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: 54.83  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288 1147 QHREQLVARVtSVDPLLDKLHGL-VLNEESYEAVRAENTNQDKMRKLFN-LSRSWSRACkDLFYQALKETH-PHLVmDLL 1223
Cdd:cd01671     3 KNRVELVEDL-DVEDILDHLIQKgVLTEEDKEEILSEKTRQDKARKLLDiLPRRGPKAF-EVFCEALRETGqPHLA-ELL 79
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 609-722 4.67e-09

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: 59.29  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  609 PITNASWEILFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPgCQLKTLWLVKCGLTSR-YCSLLASVLSAHSSLTE 687
Cdd:cd00116   176 GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASL-KSLEVLNLGDNNLTDAgAAALASALLSPNISLLT 254

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 123796288  688 LYLQLNDLGDDGVRMLCEGLRNpvcNLSILWLDLS 722
Cdd:cd00116   255 LSLSCNDITDDGAKDLAEVLAE---KESLLELDLR 286
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 365-419 2.78e-08

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: 51.41  E-value: 2.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 123796288   365 QVKALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVATFLKTGVLQKQASSLS-YSF 419
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 618-742 7.20e-07

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 52.74  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  618 LFYNLKFTRNLEGLDLSGNSLRYSV--VQSLCNTLRyPGCQLKTLWLVKCGLTSRYCSLLASVLSAhSSLTELYLQLNDL 695
Cdd:cd00116    43 LASALRPQPSLKELCLSLNETGRIPrgLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNNGL 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 123796288  696 GDDGVRMLCEGLRNPVCNLSILWLDLSSLSAQVITELRTLEEKNPKL 742
Cdd:cd00116   121 GDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDL 167
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 608-723 4.99e-06

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: 50.56  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  608 TPITNASWEILFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYpGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTE 687
Cdd:COG5238   218 NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTS 296

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 123796288  688 LYLQLNDLGDDGVRMLCEGLRNpvcNLSILWLDLSS 723
Cdd:COG5238   297 LDLSVNRIGDEGAIALAEGLQG---NKTLHTLNLAY 329
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 582-723 7.18e-06

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: 50.17  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  582 VRTLQL---NMEKQQGYALI-------SPRMVLYRWTPITNASWEILFYNLKFTRNLEGLDLSGNSL------------- 638
Cdd:COG5238   210 VTTLWLkrnPIGDEGAEILAealkgnkSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIgaegaialakalq 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  639 RYSVVQSL---CNTLRYPGC-----------QLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGDDGVRMLC 704
Cdd:COG5238   290 GNTTLTSLdlsVNRIGDEGAialaeglqgnkTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALA 369

                         170
                  ....*....|....*....
gi 123796288  705 EGLRNpvcNLSILWLDLSS 723
Cdd:COG5238   370 KYLEG---NTTLRELNLGK 385
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
682-708 5.85e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 41.24  E-value: 5.85e-05
                            10        20
                    ....*....|....*....|....*..
gi 123796288    682 HSSLTELYLQLNDLGDDGVRMLCEGLR 708
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 1142-1226 9.01e-04

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: 39.74  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288 1142 LHFMDQHREQLVARVTSVDPLLDKL-HGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1220
Cdd:cd08329     8 LSLIRKNRMALFQHLTCVLPILDHLlSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87


                  ....*.
gi 123796288 1221 DLLEKS 1226
Cdd:cd08329    88 DLFVQK 93
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
627-737 9.40e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.92  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796288  627 NLEGLDLSGNSLRySVVQSLCNtLRypgcQLKTLWLVKCGLTSrycslLASVLSAHSSLTELYLQLNDLGDdgvrmlceg 706
Cdd:COG4886   114 NLESLDLSGNQLT-DLPEELAN-LT----NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD--------- 173

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 123796288  707 LRNPVCNLSIL-WLDLSS--LSA--QVITELRTLEE 737
Cdd:COG4886   174 LPEELGNLTNLkELDLSNnqITDlpEPLGNLTNLEE 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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