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Conserved domains on  [gi|187133241|ref|NP_035002|]
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baculoviral IAP repeat-containing protein 1b [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
810-916 1.67e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


:

Pssm-ID: 436120  Cd Length: 106  Bit Score: 170.54  E-value: 1.67e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 187133241   890 GLWQLSPESFSLFISENLLRICLNFAH 916
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
508-662 3.07e-38

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: 140.90  E-value: 3.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPGQE---LAKIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGNarsLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 187133241   653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 1.89e-32

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


:

Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.89  E-value: 1.89e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187133241    159 EEARLESFEDWPFYAHgTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:smart00238    2 EEARLKTFQNWPYNSK-CTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
281-346 2.27e-27

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


:

Pssm-ID: 459891  Cd Length: 68  Bit Score: 106.20  E-value: 2.27e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241   281 RMDTFKDWPHESPGAV--EALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:pfam00653    1 RLATFENWPHSNKSPPtpEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
63-127 4.67e-23

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


:

Pssm-ID: 459891  Cd Length: 68  Bit Score: 93.88  E-value: 4.67e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187133241    63 RLKTFETY--DKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFL 127
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFL 67
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.70e-18

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 91.40  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635   106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPGQELAKIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635   185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635   258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635   329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635   407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                         410
                  ....*....|....*..
gi 187133241  794 FLAAVRLTELLSSDRQE 810
Cdd:COG5635   480 YLAARALVEELDEELLE 496
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
1106-1373 2.22e-06

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: 51.20  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1106 RLELSREDQK-LLLTLPTLQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---SKPDVLSVLPGEFPNLHHMEKL 1178
Cdd:cd00116     7 GELLKTERATeLLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116    87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFAQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116   167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1304 LqlpclrvlvfaetLDDDSVLEIAKgATRGGFQKLENLDLTLNHkITEEGYRNFFQVLDNLPNLKNLDIS 1373
Cdd:cd00116   232 N-------------LTDAGAAALAS-ALLSPNISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLR 286
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
810-916 1.67e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 170.54  E-value: 1.67e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 187133241   890 GLWQLSPESFSLFISENLLRICLNFAH 916
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
508-662 3.07e-38

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: 140.90  E-value: 3.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPGQE---LAKIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGNarsLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 187133241   653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 1.89e-32

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.89  E-value: 1.89e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187133241    159 EEARLESFEDWPFYAHgTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:smart00238    2 EEARLKTFQNWPYNSK-CTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
162-228 6.19e-32

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 119.30  E-value: 6.19e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241   162 RLESFEDWPFYAHGT-SPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQ 228
Cdd:pfam00653    1 RLATFENWPHSNKSPpTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
160-229 6.87e-31

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 116.21  E-value: 6.87e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  160 EARLESFEDWPfYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:cd00022     1 EARLKTFKNWP-ISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
281-346 2.27e-27

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 106.20  E-value: 2.27e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241   281 RMDTFKDWPHESPGAV--EALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:pfam00653    1 RLATFENWPHSNKSPPtpEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
277-346 5.27e-27

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 105.09  E-value: 5.27e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241    277 NEELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
279-346 2.09e-26

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 103.50  E-value: 2.09e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241  279 ELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:cd00022     1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
63-127 4.67e-23

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 93.88  E-value: 4.67e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187133241    63 RLKTFETY--DKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFL 127
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFL 67
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
61-129 1.23e-22

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 92.71  E-value: 1.23e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187133241   61 AKRLKTFETYDKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFLLG 129
Cdd:cd00022     1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.70e-18

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 91.40  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635   106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPGQELAKIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635   185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635   258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635   329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635   407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                         410
                  ....*....|....*..
gi 187133241  794 FLAAVRLTELLSSDRQE 810
Cdd:COG5635   480 YLAARALVEELDEELLE 496
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1106-1373 2.22e-06

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: 51.20  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1106 RLELSREDQK-LLLTLPTLQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---SKPDVLSVLPGEFPNLHHMEKL 1178
Cdd:cd00116     7 GELLKTERATeLLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116    87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFAQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116   167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1304 LqlpclrvlvfaetLDDDSVLEIAKgATRGGFQKLENLDLTLNHkITEEGYRNFFQVLDNLPNLKNLDIS 1373
Cdd:cd00116   232 N-------------LTDAGAAALAS-ALLSPNISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLR 286
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
489-611 2.89e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.08  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  489 ISQPVQGSLTIPEVFSNLNSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSI--------T 554
Cdd:cd03238     3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLidvglgylT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241  555 PGQELAKIicaqllgAGGCISEVCLSSIIQQLQHQVLFLLDDYS-GLAslPQALHTLI 611
Cdd:cd03238    81 LGQKLSTL-------SGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1155-1409 5.84e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1155 LDSKPDVLSVLPGEFPNLHHMEKLSIRTSTESDLSKLVKLIQNSPNLHVFHLKCNFLSNCEPLmtvlASCKKLREIEFSG 1234
Cdd:COG4886    47 LLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL----SNLTNLESLDLSG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1235 RCFEAMTfvNILPNFVFLKILNLRDQQFpdketsEKFAQALGSLRNLEKLFVpTGDGIHQVAKLIvrqcLQLPCLRVLvf 1314
Cdd:COG4886   123 NQLTDLP--EELANLTNLKELDLSNNQL------TDLPEPLGNLTNLKSLDL-SNNQLTDLPEEL----GNLTNLKEL-- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1315 aeTLDDDSVLEIakGATRGGFQKLENLDLTLNhKITEegyrnFFQVLDNLPNLKNLDISrhipeciqiqaitvkalGQCV 1394
Cdd:COG4886   188 --DLSNNQITDL--PEPLGNLTNLEELDLSGN-QLTD-----LPEPLANLTNLETLDLS-----------------NNQL 240
                         250
                  ....*....|....*
gi 187133241 1395 SRLPSLTRLGMLSWL 1409
Cdd:COG4886   241 TDLPELGNLTNLEEL 255
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
507-644 6.91e-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: 6.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241    507 NSVMCVEGEAGSGKTTFLKRIAFLwasgccpLLYRFQLVFYLSLSSITPGQELAKIICAQLLGAGGCISEVCLSSIIQ-- 584
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARE-------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAla 74
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187133241    585 -QLQHQVLFL-------LDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNKV---RGIRPYLDTSLEIK 644
Cdd:smart00382   75 rKLKPDVLILdeitsllDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDlgpALLRRRFDRRIVLL 145
 
Name Accession Description Interval E-value
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
810-916 1.67e-49

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 170.54  E-value: 1.67e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 187133241   890 GLWQLSPESFSLFISENLLRICLNFAH 916
Cdd:pfam17889   80 SLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
508-662 3.07e-38

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: 140.90  E-value: 3.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLyrFQLVFYLSLSSITPGQE---LAKIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGNarsLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241   585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 187133241   653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 1.89e-32

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.89  E-value: 1.89e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187133241    159 EEARLESFEDWPFYAHgTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:smart00238    2 EEARLKTFQNWPYNSK-CTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
162-228 6.19e-32

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 119.30  E-value: 6.19e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241   162 RLESFEDWPFYAHGT-SPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQ 228
Cdd:pfam00653    1 RLATFENWPHSNKSPpTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
160-229 6.87e-31

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 116.21  E-value: 6.87e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  160 EARLESFEDWPfYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLQS 229
Cdd:cd00022     1 EARLKTFKNWP-ISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
281-346 2.27e-27

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 106.20  E-value: 2.27e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241   281 RMDTFKDWPHESPGAV--EALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:pfam00653    1 RLATFENWPHSNKSPPtpEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFLK 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
277-346 5.27e-27

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 105.09  E-value: 5.27e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241    277 NEELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
279-346 2.09e-26

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 103.50  E-value: 2.09e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241  279 ELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:cd00022     1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
63-127 4.67e-23

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteriztically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 459891  Cd Length: 68  Bit Score: 93.88  E-value: 4.67e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187133241    63 RLKTFETY--DKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFL 127
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFL 67
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
61-129 1.23e-22

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 92.71  E-value: 1.23e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187133241   61 AKRLKTFETYDKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFLLG 129
Cdd:cd00022     1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.70e-18

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 91.40  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635   106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLYRfqLVFYLSLSSITPGQELAKIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635   185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635   258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635   329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635   407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                         410
                  ....*....|....*..
gi 187133241  794 FLAAVRLTELLSSDRQE 810
Cdd:COG5635   480 YLAARALVEELDEELLE 496
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1106-1373 2.22e-06

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: 51.20  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1106 RLELSREDQK-LLLTLPTLQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---SKPDVLSVLPGEFPNLHHMEKL 1178
Cdd:cd00116     7 GELLKTERATeLLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116    87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFAQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116   167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1304 LqlpclrvlvfaetLDDDSVLEIAKgATRGGFQKLENLDLTLNHkITEEGYRNFFQVLDNLPNLKNLDIS 1373
Cdd:cd00116   232 N-------------LTDAGAAALAS-ALLSPNISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLR 286
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
1114-1235 3.18e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 46.94  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1114 QKLLLTLPTLQSLEVSETNQLPDQLFHNLHKfLGLKElCVRLDSKPDVLSvlpgefpNLHHMEKLSIRTSTESDLSKLVK 1193
Cdd:cd09293     2 DPLLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIA 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 187133241 1194 LIQNSPNLHVFHLK-CNFLSNcEPLMTVLASCKKLREIEFsGR 1235
Cdd:cd09293    73 LAQSCPNLQVLDLRaCENITD-SGIVALATNCPKLQTINL-GR 113
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
489-611 2.89e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.08  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241  489 ISQPVQGSLTIPEVFSNLNSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLYRFQLVFYLSLSSI--------T 554
Cdd:cd03238     3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLidvglgylT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 187133241  555 PGQELAKIicaqllgAGGCISEVCLSSIIQQLQHQVLFLLDDYS-GLAslPQALHTLI 611
Cdd:cd03238    81 LGQKLSTL-------SGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1155-1409 5.84e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1155 LDSKPDVLSVLPGEFPNLHHMEKLSIRTSTESDLSKLVKLIQNSPNLHVFHLKCNFLSNCEPLmtvlASCKKLREIEFSG 1234
Cdd:COG4886    47 LLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL----SNLTNLESLDLSG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1235 RCFEAMTfvNILPNFVFLKILNLRDQQFpdketsEKFAQALGSLRNLEKLFVpTGDGIHQVAKLIvrqcLQLPCLRVLvf 1314
Cdd:COG4886   123 NQLTDLP--EELANLTNLKELDLSNNQL------TDLPEPLGNLTNLKSLDL-SNNQLTDLPEEL----GNLTNLKEL-- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241 1315 aeTLDDDSVLEIakGATRGGFQKLENLDLTLNhKITEegyrnFFQVLDNLPNLKNLDISrhipeciqiqaitvkalGQCV 1394
Cdd:COG4886   188 --DLSNNQITDL--PEPLGNLTNLEELDLSGN-QLTD-----LPEPLANLTNLETLDLS-----------------NNQL 240
                         250
                  ....*....|....*
gi 187133241 1395 SRLPSLTRLGMLSWL 1409
Cdd:COG4886   241 TDLPELGNLTNLEEL 255
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
507-644 6.91e-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: 6.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187133241    507 NSVMCVEGEAGSGKTTFLKRIAFLwasgccpLLYRFQLVFYLSLSSITPGQELAKIICAQLLGAGGCISEVCLSSIIQ-- 584
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARE-------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAla 74
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187133241    585 -QLQHQVLFL-------LDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNKV---RGIRPYLDTSLEIK 644
Cdd:smart00382   75 rKLKPDVLILdeitsllDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDlgpALLRRRFDRRIVLL 145
 
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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