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Conserved domains on  [gi|12656107|gb|AAK00749|]
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NAC-beta splice variant [Homo sapiens]

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 ...
 1100-1354 6.07e-147

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: 447.87  E-value: 6.07e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1100 VHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHsWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDT 1179
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1180 SLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKmIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSI 1259
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1260 RKAIDDLEMK-FQFVRIHKPPPLTPLYMGCRYTVsgSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKD 1338
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRL--SSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTD 236

                          250
                   ....*....|....*.
gi 12656107   1339 KKDETLVWEALVKPGD 1354
Cdd:pfam13553  237 KKSETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 328-497 1.92e-51

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: 178.65  E-value: 1.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    328 RIVILQGAAGIGKSTLARQVKEAWGRGQLYGDrFQHVFYFSCRELAQS-KVVSLAELIGKDGTATPAPIRQ----ILSRP 402
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    403 ERLLFILDGVDEPGWVLQEPSSelclhwsqPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFS 482
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDG--------PCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 12656107    483 ESSRKEYFYRYFTDE 497
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1380-1460 4.10e-39

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: 140.04  E-value: 4.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107 1380 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMEL 1459
Cdd:cd08330    1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                 .
gi 12656107 1460 W 1460
Cdd:cd08330   81 E 81
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 810-988 8.22e-35

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: 136.33  E-value: 8.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  810 LKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRL 889
Cdd:cd00116  110 LQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  890 RQpSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQ 969
Cdd:cd00116  190 KA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAK 268

                        170
                 ....*....|....*....
gi 12656107  970 ELRALEQEKPQLLIFSRRK 988
Cdd:cd00116  269 DLAEVLAEKESLLELDLRG 287
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 623-733 6.36e-30

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: 115.47  E-value: 6.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    623 HLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKT-------LEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLS 695
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKReslksllDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 12656107    696 QG--RNLMQWVPSL--QLLLQPHSLESLHCLYETRNKTFLTQ 733
Cdd:pfam17776   81 SEikQELLQWIKSLiqKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-88 7.38e-25

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260032  Cd Length: 84  Bit Score: 99.62  E-value: 7.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    9 LACYLEFLKKEELKEFQLLLANKAHsRSSSGETP-AQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQ 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESL-EGGLKPIPwTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKAR 79


                 .
gi 12656107   88 E 88
Cdd:cd08320   80 A 80
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 567-612 6.56e-10

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: 56.03  E-value: 6.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 12656107    567 QLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQE 612
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK 47
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 1100-1354 6.07e-147

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: 447.87  E-value: 6.07e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1100 VHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHsWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDT 1179
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1180 SLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKmIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSI 1259
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1260 RKAIDDLEMK-FQFVRIHKPPPLTPLYMGCRYTVsgSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKD 1338
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRL--SSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTD 236

                          250
                   ....*....|....*.
gi 12656107   1339 KKDETLVWEALVKPGD 1354
Cdd:pfam13553  237 KKSETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 328-497 1.92e-51

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: 178.65  E-value: 1.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    328 RIVILQGAAGIGKSTLARQVKEAWGRGQLYGDrFQHVFYFSCRELAQS-KVVSLAELIGKDGTATPAPIRQ----ILSRP 402
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    403 ERLLFILDGVDEPGWVLQEPSSelclhwsqPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFS 482
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDG--------PCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 12656107    483 ESSRKEYFYRYFTDE 497
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1380-1460 4.10e-39

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: 140.04  E-value: 4.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107 1380 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMEL 1459
Cdd:cd08330    1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                 .
gi 12656107 1460 W 1460
Cdd:cd08330   81 E 81
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 810-988 8.22e-35

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: 136.33  E-value: 8.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  810 LKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRL 889
Cdd:cd00116  110 LQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  890 RQpSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQ 969
Cdd:cd00116  190 KA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAK 268

                        170
                 ....*....|....*....
gi 12656107  970 ELRALEQEKPQLLIFSRRK 988
Cdd:cd00116  269 DLAEVLAEKESLLELDLRG 287
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 623-733 6.36e-30

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: 115.47  E-value: 6.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    623 HLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKT-------LEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLS 695
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKReslksllDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 12656107    696 QG--RNLMQWVPSL--QLLLQPHSLESLHCLYETRNKTFLTQ 733
Cdd:pfam17776   81 SEikQELLQWIKSLiqKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-88 7.38e-25

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 99.62  E-value: 7.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    9 LACYLEFLKKEELKEFQLLLANKAHsRSSSGETP-AQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQ 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESL-EGGLKPIPwTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKAR 79


                 .
gi 12656107   88 E 88
Cdd:cd08320   80 A 80
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1379-1460 6.26e-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: 88.39  E-value: 6.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1379 LHFVDQYREQLIARVTSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIM 1457
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ...
gi 12656107   1458 ELW 1460
Cdd:pfam00619   81 DLE 83
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 799-977 1.15e-20

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: 96.78  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  799 ILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLlETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLT 878
Cdd:COG5238  227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV-ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  879 DAGAKHLCQRLRQPScKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGL-RHPAckLIRLG 957
Cdd:COG5238  306 DEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT--LRELN 382

                        170       180
                 ....*....|....*....|
gi 12656107  958 LDQTTLSDEMRQELRALEQE 977
Cdd:COG5238  383 LGKNNIGKQGAEALIDALQT 402
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
281-632 1.61e-20

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 98.72  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  281 LLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFgPGLDTQEPRIVILqGAAGIGKSTLARQV-KEAWGRGQLYGD 359
Cdd:COG5635  136 LLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRL-ELLEAKKKRLLIL-GEPGSGKTTLLRYLaLELAERYLDAED 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  360 RFqhVFYFSCRELAQSKvvSLAELIGK----DGTATPAPIRQILSRPeRLLFILDGVDEpgwVLQEPSSELCLHWsqpqp 435
Cdd:COG5635  214 PI--PILIELRDLAEEA--SLEDLLAEalekRGGEPEDALERLLRNG-RLLLLLDGLDE---VPDEADRDEVLNQ----- 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  436 adalLGSLLGKtiLPEASFLITARTTALQNliPSLEQARWVEVLGFSESSRKEYFYRYFT-DERQAIRAFRLVKSNKE-- 512
Cdd:COG5635  281 ----LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDEQIEEFLKKWFEaTERKAERLLEALEENPElr 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  513 --------LWALCLVPWVS-----------WLACTCLMQQMKRKEKltltskttttlclHYLAQALQAQplgpQLRDLCS 573
Cdd:COG5635  353 elarnpllLTLLALLLRERgelpdtraelyEQFVELLLERWDEQRG-------------LTIYRELSRE----ELRELLS 415

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12656107  574 -LAAEGIWQKKTLFSPDDLRKhgldgaIISTFLKM---------------GILQEhPIPLSYSFIHLCFQEFFAA 632
Cdd:COG5635  416 eLALAMQENGRTEFAREELEE------ILREYLGRrkdaealldelllrtGLLVE-RGEGRYSFAHRSFQEYLAA 483
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-84 1.40e-16

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 75.70  E-value: 1.40e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12656107      8 RLACYLEFLKKEELKEFQLLLANKAHSRSSSgETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCA 84
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRS-IPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 567-612 6.56e-10

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: 56.03  E-value: 6.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 12656107    567 QLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQE 612
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK 47
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
921-948 1.60e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.60e-05
                            10        20
                    ....*....|....*....|....*...
gi 12656107     921 SPSLKELDLQQNNLDDVGVRLLCEGLRH 948
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
863-886 7.70e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 7.70e-05
                           10        20
                   ....*....|....*....|....
gi 12656107    863 ANQTLTELDLSFNVLTDAGAKHLC 886
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 308-416 1.36e-03

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 43.37  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   308 RGHLIE-IRDLFGPGLDTQEPriVILQGAAGIGKSTLARQvkeawgrgqlYGDRFQH----VFYFSC--RELAQSKVVSL 380
Cdd:NF040586   11 REELLErLRDQLRSGGAAVVP--QALHGLGGVGKTQLALE----------YAHRFRAdydlVWWIPAdqPELVRASLAEL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 12656107   381 AELIG-----KDGTATPAPIRQILSR---PERLLFILDGVDEPG 416
Cdd:NF040586   79 ARRLGlplgpDDVDEAARAVLDALRRgepYRRWLLVFDNADDPE 122
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 327-416 2.63e-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: 40.05  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107     327 PRIVILQGAAGIGKSTLARQVkeawgrGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAP---IRQILSRPE 403
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARAL------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGelrLRLALALAR 75

                            90
                    ....*....|....*..
gi 12656107     404 R----LLFIldgvDEPG 416
Cdd:smart00382   76 KlkpdVLIL----DEIT 88
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 322-416 4.93e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.05  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  322 LDTQEPRIVILQGAAGIGKSTLARQVkeawgrGQLYGDRFQHVFYFSCRELAQSKVVSlaeliGKDGTATPAPIRQILSR 401
Cdd:cd00009   14 LELPPPKNLLLYGPPGTGKTTLARAI------ANELFRPGAPFLYLNASDLLEGLVVA-----ELFGHFLVRLLFELAEK 82

                         90
                 ....*....|....*
gi 12656107  402 PERLLFILDGVDEPG 416
Cdd:cd00009   83 AKPGVLFIDEIDSLS 97
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 1100-1354 6.07e-147

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: 447.87  E-value: 6.07e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1100 VHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHsWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDT 1179
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1180 SLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKmIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSI 1259
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1260 RKAIDDLEMK-FQFVRIHKPPPLTPLYMGCRYTVsgSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKD 1338
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRL--SSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTD 236

                          250
                   ....*....|....*.
gi 12656107   1339 KKDETLVWEALVKPGD 1354
Cdd:pfam13553  237 KKSETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 328-497 1.92e-51

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: 178.65  E-value: 1.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    328 RIVILQGAAGIGKSTLARQVKEAWGRGQLYGDrFQHVFYFSCRELAQS-KVVSLAELIGKDGTATPAPIRQ----ILSRP 402
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    403 ERLLFILDGVDEPGWVLQEPSSelclhwsqPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFS 482
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDG--------PCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 12656107    483 ESSRKEYFYRYFTDE 497
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1380-1460 4.10e-39

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: 140.04  E-value: 4.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107 1380 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMEL 1459
Cdd:cd08330    1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                 .
gi 12656107 1460 W 1460
Cdd:cd08330   81 E 81
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 810-988 8.22e-35

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: 136.33  E-value: 8.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  810 LKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRL 889
Cdd:cd00116  110 LQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  890 RQpSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQ 969
Cdd:cd00116  190 KA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAK 268

                        170
                 ....*....|....*....
gi 12656107  970 ELRALEQEKPQLLIFSRRK 988
Cdd:cd00116  269 DLAEVLAEKESLLELDLRG 287
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 800-959 1.89e-31

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: 126.32  E-value: 1.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  800 LFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRpRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTD 879
Cdd:cd00116  157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  880 AGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLD 959
Cdd:cd00116  236 AGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 623-733 6.36e-30

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: 115.47  E-value: 6.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    623 HLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKT-------LEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLS 695
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKReslksllDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 12656107    696 QG--RNLMQWVPSL--QLLLQPHSLESLHCLYETRNKTFLTQ 733
Cdd:pfam17776   81 SEikQELLQWIKSLiqKELSSERFLNLFHCLYELQDESFVKE 122
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 802-966 1.12e-26

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: 112.45  E-value: 1.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  802 SVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLET-------------LRLAGCGLTAE------DCKDLAFG-- 860
Cdd:cd00116   17 ELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELclslnetgriprgLQSLLQGLTKGcglqelDLSDNALGpd 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  861 -------LRANQTLTELDLSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNN 933
Cdd:cd00116   97 gcgvlesLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNG 176

                        170       180       190
                 ....*....|....*....|....*....|...
gi 12656107  934 LDDVGVRLLCEGLRHpACKLIRLGLDQTTLSDE 966
Cdd:cd00116  177 IGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-88 7.38e-25

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 99.62  E-value: 7.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    9 LACYLEFLKKEELKEFQLLLANKAHsRSSSGETP-AQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQ 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESL-EGGLKPIPwTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKAR 79


                 .
gi 12656107   88 E 88
Cdd:cd08320   80 A 80
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 9-87 6.52e-23

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 93.52  E-value: 6.52e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12656107    9 LACYLEFLKKEELKEFQLLLANKahsrsSSGETPAQPEKTsGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQ 87
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASE-----LKLTRKMQEEYD-RIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1379-1460 6.26e-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: 88.39  E-value: 6.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   1379 LHFVDQYREQLIARVTSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIM 1457
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ...
gi 12656107   1458 ELW 1460
Cdd:pfam00619   81 DLE 83
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 799-977 1.15e-20

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: 96.78  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  799 ILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLlETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLT 878
Cdd:COG5238  227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV-ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  879 DAGAKHLCQRLRQPScKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGL-RHPAckLIRLG 957
Cdd:COG5238  306 DEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT--LRELN 382

                        170       180
                 ....*....|....*....|
gi 12656107  958 LDQTTLSDEMRQELRALEQE 977
Cdd:COG5238  383 LGKNNIGKQGAEALIDALQT 402
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
281-632 1.61e-20

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 98.72  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  281 LLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFgPGLDTQEPRIVILqGAAGIGKSTLARQV-KEAWGRGQLYGD 359
Cdd:COG5635  136 LLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRL-ELLEAKKKRLLIL-GEPGSGKTTLLRYLaLELAERYLDAED 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  360 RFqhVFYFSCRELAQSKvvSLAELIGK----DGTATPAPIRQILSRPeRLLFILDGVDEpgwVLQEPSSELCLHWsqpqp 435
Cdd:COG5635  214 PI--PILIELRDLAEEA--SLEDLLAEalekRGGEPEDALERLLRNG-RLLLLLDGLDE---VPDEADRDEVLNQ----- 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  436 adalLGSLLGKtiLPEASFLITARTTALQNliPSLEQARWVEVLGFSESSRKEYFYRYFT-DERQAIRAFRLVKSNKE-- 512
Cdd:COG5635  281 ----LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDEQIEEFLKKWFEaTERKAERLLEALEENPElr 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  513 --------LWALCLVPWVS-----------WLACTCLMQQMKRKEKltltskttttlclHYLAQALQAQplgpQLRDLCS 573
Cdd:COG5635  353 elarnpllLTLLALLLRERgelpdtraelyEQFVELLLERWDEQRG-------------LTIYRELSRE----ELRELLS 415

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12656107  574 -LAAEGIWQKKTLFSPDDLRKhgldgaIISTFLKM---------------GILQEhPIPLSYSFIHLCFQEFFAA 632
Cdd:COG5635  416 eLALAMQENGRTEFAREELEE------ILREYLGRrkdaealldelllrtGLLVE-RGEGRYSFAHRSFQEYLAA 483
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 790-977 2.66e-19

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: 92.55  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  790 VPVTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRClLETLRLAGCGLTAEDCKDLAFGLRANQTLTE 869
Cdd:COG5238  246 NQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTT-LTSLDLSVNRIGDEGAIALAEGLQGNKTLHT 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  870 LDLSFNVLTDAGAKHLCQRLrQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHP 949
Cdd:COG5238  325 LNLAYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN 403

                        170       180
                 ....*....|....*....|....*...
gi 12656107  950 acKLIRLGLDQTTLSDEMRQELRALEQE 977
Cdd:COG5238  404 --RLHTLILDGNLIGAEAQQRLEQLLER 429
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-84 1.40e-16

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 75.70  E-value: 1.40e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12656107      8 RLACYLEFLKKEELKEFQLLLANKAHSRSSSgETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCA 84
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRS-IPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 792-904 1.27e-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: 76.63  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  792 VTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELD 871
Cdd:cd00116  205 LTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELD 284

                         90       100       110
                 ....*....|....*....|....*....|...
gi 12656107  872 LSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSC 904
Cdd:cd00116  285 LRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 1384-1455 6.38e-10

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: 56.76  E-value: 6.38e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12656107 1384 QYREQLIARVtSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETH-PHL 1455
Cdd:cd01671    3 KNRVELVEDL-DVEDILDHLIQkGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHL 75
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 567-612 6.56e-10

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: 56.03  E-value: 6.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 12656107    567 QLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQE 612
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK 47
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
808-937 2.49e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.10  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  808 RNLKELDLSGNSLSH--SAVKSLCKtlrrprclLETLRLAGCGLTaedckDLAFGLRANQTLTELDLSFNVLTDAGAKhl 885
Cdd:COG4886  136 TNLKELDLSNNQLTDlpEPLGNLTN--------LKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLPEP-- 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 12656107  886 cqrLRQPScKLQRLQLVSCGLTsdccqDLASVLSASPSLKELDLQQNNLDDV 937
Cdd:COG4886  201 ---LGNLT-NLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTDL 243
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
809-965 7.81e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  809 NLKELDLSGNSLShsavkSLCKTLRRPRCLlETLRLAGCGLTaedckDLAFGLRANQTLTELDLSFNVLTDAGAkHLCQr 888
Cdd:COG4886  114 NLESLDLSGNQLT-----DLPEELANLTNL-KELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTDLPE-ELGN- 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12656107  889 LRqpscKLQRLQLVSCGLTsdccqDLASVLSASPSLKELDLQQNNLDDVGVRLlcEGLRhpacKLIRLGLDQTTLSD 965
Cdd:COG4886  181 LT----NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLT----NLETLDLSNNQLTD 242
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 714-975 1.56e-08

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: 58.65  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  714 HSLESLHC------LYETRNKTFLTQVMAH-----FEEMGMCVETDMELLVctfcIKFSRHVKKLQLIEGRQH------- 775
Cdd:COG5238   43 HGGAILLArylqsrSSITQYLRFEGQGDPGlnpvaLEKAAEAFPTQLLVVD----WEGAEEVSPVALAETATAvatpppd 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  776 -RSTWSPTMVVLFRWVPVTDAYwQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDC 854
Cdd:COG5238  119 lRRIMAKTLEDSLILYLALPRR-INLIQVLKDPLGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  855 KDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRLR---------------------------QPSCKLQRLQLVSCGLT 907
Cdd:COG5238  198 EELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKgnkslttldlsnnqigdegvialaealKNNTTVETLYLSGNQIG 277

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12656107  908 SDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPAcKLIRLGLDQTTLSD-------EMRQELRALE 975
Cdd:COG5238  278 AEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAqgaialaKALQENTTLH 351
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
809-983 1.92e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  809 NLKELDLSGNSLSH--SAVKSLCKtlrrprclLETLRLAGCGLTaedckDLAFGLRANQTLTELDLSFNVLTDAGAKhlc 886
Cdd:COG4886  160 NLKSLDLSNNQLTDlpEELGNLTN--------LKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTDLPEP--- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  887 qrLRQPScKLQRLQLVSCGLTsdccqDLASvLSASPSLKELDLQQNNLDDVGVrllCEGLRhpacKLIRLGLDQTTLSDE 966
Cdd:COG4886  224 --LANLT-NLETLDLSNNQLT-----DLPE-LGNLTNLEELDLSNNQLTDLPP---LANLT----NLKTLDLSNNQLTDL 287

                        170
                 ....*....|....*..
gi 12656107  967 MRQELRALEQEKPQLLI 983
Cdd:COG4886  288 KLKELELLLGLNSLLLL 304
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
809-978 8.13e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 8.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  809 NLKELDLSGNSLS--HSAVKSLCKtlrrprclLETLRLAGCGLTaedckDLAFGLRANQTLTELDLSFNVLTDAGAkhlc 886
Cdd:COG4886  183 NLKELDLSNNQITdlPEPLGNLTN--------LEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTDLPE---- 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  887 qrLRQPScKLQRLQLVSCGLTSdccqdlASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDE 966
Cdd:COG4886  246 --LGNLT-NLEELDLSNNQLTD------LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLIL 316

                        170
                 ....*....|..
gi 12656107  967 MRQELRALEQEK 978
Cdd:COG4886  317 LLLLTTLLLLLL 328
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
921-948 1.60e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.60e-05
                            10        20
                    ....*....|....*....|....*...
gi 12656107     921 SPSLKELDLQQNNLDDVGVRLLCEGLRH 948
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 792-890 3.45e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 48.25  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  792 VTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLEtLRLAGCGLTAEDCKDLAFGLRANQtLTELD 871
Cdd:COG5238  332 IGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRE-LNLGKNNIGKQGAEALIDALQTNR-LHTLI 409

                         90       100
                 ....*....|....*....|..
gi 12656107  872 LSFNVLTDAGAKHL---CQRLR 890
Cdd:COG5238  410 LDGNLIGAEAQQRLeqlLERIK 431
LRR_6 pfam13516
Leucine Rich repeat;
863-886 7.70e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 7.70e-05
                           10        20
                   ....*....|....*....|....
gi 12656107    863 ANQTLTELDLSFNVLTDAGAKHLC 886
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 308-399 1.58e-04

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: 44.03  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107    308 RGHLIE-IRDLFGPgLDTQEPRIVILQGAAGIGKSTLARQVKEAW---GRGQLYGDRFQHVFYFSCRElAQSKVVSLAEL 383
Cdd:pfam13191    5 REEELEqLLDALDR-VRSGRPPSVLLTGEAGTGKTTLLRELLRALerdGGYFLRGKCDENLPYSPLLE-ALTREGLLRQL 82

                           90
                   ....*....|....*.
gi 12656107    384 IGKDGTATPAPIRQIL 399
Cdd:pfam13191   83 LDELESSLLEAWRAAL 98
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
793-965 3.81e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  793 TDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLlETLRLAGCGltaedckdlafGLRANQTLTELDL 872
Cdd:COG4886   53 LSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNL-TELDLSGNE-----------ELSNLTNLESLDL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  873 SFNVLTDagakhLCQRLRQPScKLQRLQLVSCGLTsdccqDLASVLSASPSLKELDLQQNNLDDVGVRLlcEGLRhpacK 952
Cdd:COG4886  121 SGNQLTD-----LPEELANLT-NLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTDLPEEL--GNLT----N 183

                        170
                 ....*....|...
gi 12656107  953 LIRLGLDQTTLSD 965
Cdd:COG4886  184 LKELDLSNNQITD 196
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
864-891 8.03e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.16  E-value: 8.03e-04
                            10        20
                    ....*....|....*....|....*...
gi 12656107     864 NQTLTELDLSFNVLTDAGAKHLCQRLRQ 891
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 308-416 1.36e-03

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 43.37  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   308 RGHLIE-IRDLFGPGLDTQEPriVILQGAAGIGKSTLARQvkeawgrgqlYGDRFQH----VFYFSC--RELAQSKVVSL 380
Cdd:NF040586   11 REELLErLRDQLRSGGAAVVP--QALHGLGGVGKTQLALE----------YAHRFRAdydlVWWIPAdqPELVRASLAEL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 12656107   381 AELIG-----KDGTATPAPIRQILSR---PERLLFILDGVDEPG 416
Cdd:NF040586   79 ARRLGlplgpDDVDEAARAVLDALRRgepYRRWLLVFDNADDPE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 12-88 2.15e-03

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 38.27  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107   12 YLEFLKKEELKEFQLLLAN---KAHSRSSSGETpaqpEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQE 88
Cdd:cd08321    7 ALEDLGEEELKKFKWKLRDiplEGYPRIPRGKL----ENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 327-416 2.63e-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: 40.05  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107     327 PRIVILQGAAGIGKSTLARQVkeawgrGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAP---IRQILSRPE 403
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARAL------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGelrLRLALALAR 75

                            90
                    ....*....|....*..
gi 12656107     404 R----LLFIldgvDEPG 416
Cdd:smart00382   76 KlkpdVLIL----DEIT 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 808-978 3.34e-03

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.54  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  808 RNLKELDLSGNSLSHsaVKSL--CKTLR-----------------RPRCL------LETLRLAGCGLTaeDCKDLAfGLR 862
Cdd:cd21340   68 VNLKKLYLGGNRISV--VEGLenLTNLEelhienqrlppgekltfDPRSLaalsnsLRVLNISGNNID--SLEPLA-PLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  863 AnqtLTELDLSFNVLTDAgakhlcqrlrqpscklqrlqlvscgltsdccQDLASVLSASPSLKELDLQQNnlddvgvrll 942
Cdd:cd21340  143 N---LEQLDASNNQISDL-------------------------------EELLDLLSSWPSLRELDLTGN---------- 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 12656107  943 ceglrhPACKLIRLG------------LDQTTLSDEMRQELRALEQEK 978
Cdd:cd21340  179 ------PVCKKPKYRdkiilaskslevLDGKEITDTERQFLKRLKARK 220
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 322-416 4.93e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.05  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12656107  322 LDTQEPRIVILQGAAGIGKSTLARQVkeawgrGQLYGDRFQHVFYFSCRELAQSKVVSlaeliGKDGTATPAPIRQILSR 401
Cdd:cd00009   14 LELPPPKNLLLYGPPGTGKTTLARAI------ANELFRPGAPFLYLNASDLLEGLVVA-----ELFGHFLVRLLFELAEK 82

                         90
                 ....*....|....*
gi 12656107  402 PERLLFILDGVDEPG 416
Cdd:cd00009   83 AKPGVLFIDEIDSLS 97
 
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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