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Conserved domains on  [gi|110665740|ref|NP_001035786|]
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NACHT, LRR and PYD domains-containing protein 1b allele 2 isoform 1 [Mus musculus]

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 ...
 812-1064 1.95e-141

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: 427.07  E-value: 1.95e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   812 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 891
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   892 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 971
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   972 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1050
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 110665740  1051 HMKLIWEALLKPGD 1064
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 131-297 1.42e-42

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: 152.84  E-value: 1.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   131 QLVIIEGAAGIGKSTLARQVKRAWKEGQLYRNhFQHVFFLSCRELAQYE-QLSLAELIAQGQEVPTVPIRQ----ILSHP 205
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   206 KELLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPGASFLLTARTTALQKIIPYVGQPRRVEVLGFS 285
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|..
gi 110665740   286 KFEREVYFRKYF 297
Cdd:pfam05729  152 ESDRKQYVRKYF 163
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1084-1164 4.40e-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: 4.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740 1084 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1163
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 110665740 1164 L 1164
Cdd:cd08330    81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 426-535 4.31e-22

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: 92.74  E-value: 4.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   426 HLCLQEFFAVMSYILEDSDERCD------GMEFKRTVETLI-EVYGRHTLCEEPTVHFLFGLVNEQGMREMKKIFDCKLP 498
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNplkeffGLRKRESLKSLLdKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 110665740   499 LGTELKMLKSTL----GNPTYQHHLGLLHCLYESQEEVLLT 535
Cdd:pfam17776   81 SEIKQELLQWIKsliqKELSSERFLNLFHCLYELQDESFVK 121
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 592-721 9.51e-14

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: 73.54  E-value: 9.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  592 KGQQGHKLTVASMVLYRWTpITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYpGCQLKTLWLVECGLTP 671
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNR-LEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110665740  672 TYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRACNLRILRL 721
Cdd:cd00116   208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 370-424 1.46e-04

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: 40.63  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110665740   370 QLRALCSLAAEGICQRRTLFSESDLCKQGLAEDAIATFLKIGILQKQASSLS-YSF 424
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 ...
 812-1064 1.95e-141

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: 427.07  E-value: 1.95e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   812 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 891
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   892 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 971
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   972 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1050
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 110665740  1051 HMKLIWEALLKPGD 1064
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 131-297 1.42e-42

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: 152.84  E-value: 1.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   131 QLVIIEGAAGIGKSTLARQVKRAWKEGQLYRNhFQHVFFLSCRELAQYE-QLSLAELIAQGQEVPTVPIRQ----ILSHP 205
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   206 KELLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPGASFLLTARTTALQKIIPYVGQPRRVEVLGFS 285
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|..
gi 110665740   286 KFEREVYFRKYF 297
Cdd:pfam05729  152 ESDRKQYVRKYF 163
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1084-1164 4.40e-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: 4.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740 1084 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1163
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 110665740 1164 L 1164
Cdd:cd08330    81 E 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
127-434 1.73e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  127 HKKPQLVIIeGAAGIGKSTLARQV-KRAWKEGQLYRNHFqhVFFLSCRELAqyEQLSLAELIAQ---GQEVPTVP-IRQI 201
Cdd:COG5635   178 AKKKRLLIL-GEPGSGKTTLLRYLaLELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEaleKRGGEPEDaLERL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  202 LSHPKeLLFILDGIDEpawvLADQNpelclhwsQRQPVHTLLGSLLGKsiLPGASFLLTARTTALQKIipYVGQPRRVEV 281
Cdd:COG5635   253 LRNGR-LLLLLDGLDE----VPDEA--------DRDEVLNQLRRFLER--YPKARVIITSRPEGYDSS--ELEGFEVLEL 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  282 LGFSKFEREVYFRKYFVKESDAIAAF----------RLVVSNPVLLT-LCEVpwvcwlvctclkkqMEQGGELsltSQTT 350
Cdd:COG5635   316 APLSDEQIEEFLKKWFEATERKAERLlealeenpelRELARNPLLLTlLALL--------------LRERGEL---PDTR 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  351 TALCLKYL-----------SLTIPGQHMRTQLRALCS-LAAEGICQRRTLFSESD--------LCKQGLAEDAIATFL-K 409
Cdd:COG5635   379 AELYEQFVelllerwdeqrGLTIYRELSREELRELLSeLALAMQENGRTEFAREEleeilreyLGRRKDAEALLDELLlR 458

                         330       340
                  ....*....|....*....|....*
gi 110665740  410 IGILQKQASSlSYSFAHLCLQEFFA 434
Cdd:COG5635   459 TGLLVERGEG-RYSFAHRSFQEYLA 482
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 426-535 4.31e-22

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: 92.74  E-value: 4.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   426 HLCLQEFFAVMSYILEDSDERCD------GMEFKRTVETLI-EVYGRHTLCEEPTVHFLFGLVNEQGMREMKKIFDCKLP 498
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNplkeffGLRKRESLKSLLdKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 110665740   499 LGTELKMLKSTL----GNPTYQHHLGLLHCLYESQEEVLLT 535
Cdd:pfam17776   81 SEIKQELLQWIKsliqKELSSERFLNLFHCLYELQDESFVK 121
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1083-1163 3.11e-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: 88.77  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  1083 LHFMDQHREQLVARVTSVDPLLDKLHG-LVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1161
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 110665740  1162 DL 1163
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 592-721 9.51e-14

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 73.54  E-value: 9.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  592 KGQQGHKLTVASMVLYRWTpITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYpGCQLKTLWLVECGLTP 671
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNR-LEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110665740  672 TYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRACNLRILRL 721
Cdd:cd00116   208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 600-749 1.13e-07

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: 55.57  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  600 TVASMVLYRwTPITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYpGCQLKTLWLVECGLTPTYCSLLAS 679
Cdd:COG5238   209 TVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAK 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110665740  680 VLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRAcNLRILRLDLYSLSAQ-VITELRTLEEN----NLKLHISSI 749
Cdd:COG5238   287 ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQgAIALAKALQENttlhSLDLSDNQI 360
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
685-710 1.32e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 110665740    685 SSLRELDLQLNDLCDDGVRMLCEGLR 710
Cdd:smart00368    2 PSLRELDLSNNKLGDEGARALAEALK 27
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 370-424 1.46e-04

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: 40.63  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110665740   370 QLRALCSLAAEGICQRRTLFSESDLCKQGLAEDAIATFLKIGILQKQASSLS-YSF 424
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 129-218 5.43e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 5.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740    129 KPQLVIIEGAAGIGKSTLARQVKRawkegQLYRNHFQhVFFLSCRELAQYEQLSLAELIAQGQEVPTVPIRQI------- 201
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALAR-----ELGPPGGG-VIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlalala 74

                            90
                    ....*....|....*..
gi 110665740    202 LSHPKELLFildgIDEP 218
Cdd:smart00382   75 RKLKPDVLI----LDEI 87
LRR_6 pfam13516
Leucine Rich repeat;
683-706 7.75e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 7.75e-03
                           10        20
                   ....*....|....*....|....
gi 110665740   683 ACSSLRELDLQLNDLCDDGVRMLC 706
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 812-1064 1.95e-141

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: 427.07  E-value: 1.95e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   812 VQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPlQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKAST 891
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLP-PQHWMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   892 FDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIiPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTI 971
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   972 QKAIDDEEMK-FQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKK 1050
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 110665740  1051 HMKLIWEALLKPGD 1064
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 131-297 1.42e-42

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: 152.84  E-value: 1.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   131 QLVIIEGAAGIGKSTLARQVKRAWKEGQLYRNhFQHVFFLSCRELAQYE-QLSLAELIAQGQEVPTVPIRQ----ILSHP 205
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   206 KELLFILDGIDEPAWVLADQNPElclhwsqrQPVHTLLGSLLGKSILPGASFLLTARTTALQKIIPYVGQPRRVEVLGFS 285
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|..
gi 110665740   286 KFEREVYFRKYF 297
Cdd:pfam05729  152 ESDRKQYVRKYF 163
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1084-1164 4.40e-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: 4.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740 1084 HFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDL 1163
Cdd:cd08330     1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                  .
gi 110665740 1164 L 1164
Cdd:cd08330    81 E 81
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
127-434 1.73e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  127 HKKPQLVIIeGAAGIGKSTLARQV-KRAWKEGQLYRNHFqhVFFLSCRELAqyEQLSLAELIAQ---GQEVPTVP-IRQI 201
Cdd:COG5635   178 AKKKRLLIL-GEPGSGKTTLLRYLaLELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEaleKRGGEPEDaLERL 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  202 LSHPKeLLFILDGIDEpawvLADQNpelclhwsQRQPVHTLLGSLLGKsiLPGASFLLTARTTALQKIipYVGQPRRVEV 281
Cdd:COG5635   253 LRNGR-LLLLLDGLDE----VPDEA--------DRDEVLNQLRRFLER--YPKARVIITSRPEGYDSS--ELEGFEVLEL 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  282 LGFSKFEREVYFRKYFVKESDAIAAF----------RLVVSNPVLLT-LCEVpwvcwlvctclkkqMEQGGELsltSQTT 350
Cdd:COG5635   316 APLSDEQIEEFLKKWFEATERKAERLlealeenpelRELARNPLLLTlLALL--------------LRERGEL---PDTR 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  351 TALCLKYL-----------SLTIPGQHMRTQLRALCS-LAAEGICQRRTLFSESD--------LCKQGLAEDAIATFL-K 409
Cdd:COG5635   379 AELYEQFVelllerwdeqrGLTIYRELSREELRELLSeLALAMQENGRTEFAREEleeilreyLGRRKDAEALLDELLlR 458

                         330       340
                  ....*....|....*....|....*
gi 110665740  410 IGILQKQASSlSYSFAHLCLQEFFA 434
Cdd:COG5635   459 TGLLVERGEG-RYSFAHRSFQEYLA 482
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 426-535 4.31e-22

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: 92.74  E-value: 4.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   426 HLCLQEFFAVMSYILEDSDERCD------GMEFKRTVETLI-EVYGRHTLCEEPTVHFLFGLVNEQGMREMKKIFDCKLP 498
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNplkeffGLRKRESLKSLLdKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 110665740   499 LGTELKMLKSTL----GNPTYQHHLGLLHCLYESQEEVLLT 535
Cdd:pfam17776   81 SEIKQELLQWIKsliqKELSSERFLNLFHCLYELQDESFVK 121
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1083-1163 3.11e-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: 88.77  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  1083 LHFMDQHREQLVARVTSVDPLLDKLHG-LVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1161
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 110665740  1162 DL 1163
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 592-721 9.51e-14

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 73.54  E-value: 9.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  592 KGQQGHKLTVASMVLYRWTpITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYpGCQLKTLWLVECGLTP 671
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNR-LEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTD 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110665740  672 TYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRACNLRILRL 721
Cdd:cd00116   208 EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 624-722 4.11e-13

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: 71.62  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  624 LKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYPGCQLKTLWLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCDDGVR 703
Cdd:cd00116   217 LASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                          90
                  ....*....|....*....
gi 110665740  704 MLCEGLRNRACNLRILRLD 722
Cdd:cd00116   297 LLAESLLEPGNELESLWVK 315
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 620-742 9.79e-13

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: 70.46  E-value: 9.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  620 LFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYPGCQLKTLWLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCD 699
Cdd:cd00116   100 VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGD 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 110665740  700 DGVRMLCEGLRNRaCNLRILRLDLYSLS-------AQVITELRTLEENNL 742
Cdd:cd00116   180 AGIRALAEGLKAN-CNLEVLDLNNNGLTdegasalAETLASLKSLEVLNL 228
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 1088-1164 4.65e-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: 54.06  E-value: 4.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740 1088 QHREQLVARVtSVDPLLDKLHGL-VLNEESYEAVRAENTNQDKMRKLFN-LSRSWSRACkDLFYQALKETH-PHLVmDLL 1164
Cdd:cd01671     3 KNRVELVEDL-DVEDILDHLIQKgVLTEEDKEEILSEKTRQDKARKLLDiLPRRGPKAF-EVFCEALRETGqPHLA-ELL 79
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 618-742 1.69e-08

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: 57.75  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  618 KILFYNLKFNSNLEGLDLSGNPL--SYSAVQYLCDAMIyPGCQLKTLWLVECGLTPTYCSLLASVLSAcSSLRELDLQLN 695
Cdd:cd00116    41 KALASALRPQPSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNN 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110665740  696 DLCDDGVRMLCEGLRNRACNLRILRLDLYSLS-------AQVITELRTLEENNL 742
Cdd:cd00116   119 GLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEgascealAKALRANRDLKELNL 172
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 600-749 1.13e-07

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: 55.57  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  600 TVASMVLYRwTPITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYpGCQLKTLWLVECGLTPTYCSLLAS 679
Cdd:COG5238   209 TVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAK 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110665740  680 VLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRAcNLRILRLDLYSLSAQ-VITELRTLEEN----NLKLHISSI 749
Cdd:COG5238   287 ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQgAIALAKALQENttlhSLDLSDNQI 360
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 627-724 2.57e-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: 51.33  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  627 NSNLEGLDLSGNPLSYSAVQYLCDAMIyPGCQLKTLWLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLC 706
Cdd:COG5238   179 NNSVETVYLGCNQIGDEGIEELAEALT-QNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                          90
                  ....*....|....*...
gi 110665740  707 EGLRNracNLRILRLDLY 724
Cdd:COG5238   258 EALKN---NTTVETLYLS 272
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
685-710 1.32e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 110665740    685 SSLRELDLQLNDLCDDGVRMLCEGLR 710
Cdd:smart00368    2 PSLRELDLSNNKLGDEGARALAEALK 27
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 370-424 1.46e-04

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: 40.63  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110665740   370 QLRALCSLAAEGICQRRTLFSESDLCKQGLAEDAIATFLKIGILQKQASSLS-YSF 424
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 610-743 6.08e-04

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 43.63  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  610 TPITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAM-----------------------IYPGCQ----LKTL 662
Cdd:COG5238   246 NQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgnttltsldlsvnrigdegaiaLAEGLQgnktLHTL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  663 WLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRAcNLRILRL---DLYSLSAQVITELrtLEE 739
Cdd:COG5238   326 NLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLgknNIGKQGAEALIDA--LQT 402


                  ....
gi 110665740  740 NNLK 743
Cdd:COG5238   403 NRLH 406
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 1083-1167 8.90e-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: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740 1083 LHFMDQHREQLVARVTSVDPLLDKL-HGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVM 1161
Cdd:cd08329     8 LSLIRKNRMALFQHLTCVLPILDHLlSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87


                  ....*.
gi 110665740 1162 DLLEKS 1167
Cdd:cd08329    88 DLFVQK 93
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 110-259 1.83e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.56  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740   110 RGHMIE-IQDLFGPNRgtHKKPQLVIIEGAAGIGKSTLARQVKRAWKEgqlyrnHFQHVFFLSCRELAQYeqLSLAELIA 188
Cdd:pfam13191    5 REEELEqLLDALDRVR--SGRPPSVLLTGEAGTGKTTLLRELLRALER------DGGYFLRGKCDENLPY--SPLLEALT 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110665740   189 QGQEvptvpIRQILSHPKELLFILDGIDEPAWVLADQNpelcLHWSQRQPVHTLLGSLLGKSILPGASFLL 259
Cdd:pfam13191   75 REGL-----LRQLLDELESSLLEAWRAALLEALAPVPE----LPGDLAERLLDLLLRLLDLLARGERPLVL 136
COG3899 COG3899
Predicted ATPase [General function prediction only];
130-220 2.20e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740  130 PQLVIIEGAAGIGKSTLARQVKRAWKEgqlyrnhfQHVFFLSCRelaqYEQLslaeliaqGQEVPTVPIRQILshpKELL 209
Cdd:COG3899   311 GELVLVSGEAGIGKSRLVRELARRARA--------RGGRVLRGK----CDQL--------ERGVPYAPLAQAL---RALL 367

                          90
                  ....*....|.
gi 110665740  210 FILDGIDEPAW 220
Cdd:COG3899   368 GQLPEDELAAW 378
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 129-218 5.43e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.89  E-value: 5.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110665740    129 KPQLVIIEGAAGIGKSTLARQVKRawkegQLYRNHFQhVFFLSCRELAQYEQLSLAELIAQGQEVPTVPIRQI------- 201
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALAR-----ELGPPGGG-VIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlalala 74

                            90
                    ....*....|....*..
gi 110665740    202 LSHPKELLFildgIDEP 218
Cdd:smart00382   75 RKLKPDVLI----LDEI 87
LRR_6 pfam13516
Leucine Rich repeat;
683-706 7.75e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 7.75e-03
                           10        20
                   ....*....|....*....|....
gi 110665740   683 ACSSLRELDLQLNDLCDDGVRMLC 706
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
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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