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Conserved domains on  [gi|26050064|gb|AAN77911|]
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BIRC1B protein [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 3.04e-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: 170.16  E-value: 3.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDENESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 26050064    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 1.07e-39

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: 145.14  E-value: 1.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLnrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 26050064    653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 2.36e-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: 120.50  E-value: 2.36e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26050064     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 2.48e-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: 105.82  E-value: 2.48e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064    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 5.15e-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: 5.15e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26050064     63 RLKTFETY--DKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFL 127
Cdd:pfam00653    1 RLATFENWphSNKSPPTPEELAEAGFYYTGTGDRVQCFYCGLELDGWEEGDDPWEEHKKHSPDCPFL 67
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.10e-19

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 94.87  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635  106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLNRfqLVFYLSLSSITPDQGLANIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635  185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635  258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635  329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635  407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                        410
                 ....*....|....*..
gi 26050064  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 1.17e-05

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: 49.28  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1106 RLELSRED-QELLLTLPALQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---GKPNVLSVLPREFPNLHHMEKL 1178
Cdd:cd00116    7 GELLKTERaTELLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116   87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFGQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116  167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 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 3.04e-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: 170.16  E-value: 3.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDENESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 26050064    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 1.07e-39

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: 145.14  E-value: 1.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLnrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 26050064    653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 2.36e-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: 120.50  E-value: 2.36e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26050064     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 6.96e-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: 118.92  E-value: 6.96e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064    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 8.42e-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: 115.83  E-value: 8.42e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  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 2.48e-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: 105.82  E-value: 2.48e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064    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 6.28e-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: 6.28e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064     277 NEELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
279-346 2.45e-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: 103.11  E-value: 2.45e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064  279 ELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
63-127 5.15e-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: 5.15e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26050064     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 1.41e-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: 92.33  E-value: 1.41e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26050064   61 AKRLKTFETYDKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFLLG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.10e-19

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 94.87  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635  106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLNRfqLVFYLSLSSITPDQGLANIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635  185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635  258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635  329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635  407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                        410
                 ....*....|....*..
gi 26050064  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 1.17e-05

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: 49.28  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1106 RLELSRED-QELLLTLPALQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---GKPNVLSVLPREFPNLHHMEKL 1178
Cdd:cd00116    7 GELLKTERaTELLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116   87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFGQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116  167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1304 LqlpclrvlvfaetLDDDSVLEIAKgATRGGFQKLENLDLTLNHkITEEGYRNFFQVLDNLPNLKNLDIS 1373
Cdd:cd00116  232 N-------------LTDAGAAALAS-ALLSPNISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLR 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1091-1347 1.67e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1091 ALELSKASVTKCSMSRLELSREDQELLLTLPALQSLEVSETNQLPDQLFHNLHKFLGLKEL--CVRLDGKPNVLSVLPRE 1168
Cdd:COG4886   52 LLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLtnLESLDLSGNQLTDLPEE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1169 FPNLHHMEKLSIRtstESDLSKLVKLIQNSPNLHVFHLKCNFLSNcepLMTVLASCKKLREIEFSGRCFEAMTFVniLPN 1248
Cdd:COG4886  132 LANLTNLKELDLS---NNQLTDLPEPLGNLTNLKSLDLSNNQLTD---LPEELGNLTNLKELDLSNNQITDLPEP--LGN 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1249 FVFLKILNLRDQQFpdketsEKFGQALGSLRNLEKLFVpTGDGIHQVAKLivrqcLQLPCLRVLVFAETldddsvlEIAK 1328
Cdd:COG4886  204 LTNLEELDLSGNQL------TDLPEPLANLTNLETLDL-SNNQLTDLPEL-----GNLTNLEELDLSNN-------QLTD 264
                        250
                 ....*....|....*....
gi 26050064 1329 GATRGGFQKLENLDLTLNH 1347
Cdd:COG4886  265 LPPLANLTNLKTLDLSNNQ 283
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
489-611 5.47e-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: 42.31  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  489 ISQPVQGSLTIPEVFSNLNSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLNRFQLVFYLSLSSITpDQGLANI 562
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26050064  563 ICAQLLG--AGGCISEVCLSSIIQQLQHQVLFLLDDYS-GLAslPQALHTLI 611
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
 
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 3.04e-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: 170.16  E-value: 3.04e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    810 EDQDLGLYYLRQINSPLKAMSIYHTFLKYvSSHPSSKAAPTVVSHLLQLVDENESLENMSENEDYMKLHPEALLWIECLR 889
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLY-TCHSSTKAGPKIVSHLLHLVDHKESLENLSENDDYLKHHPETSLLMQNIR 79
                           90       100
                   ....*....|....*....|....*..
gi 26050064    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 1.07e-39

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: 145.14  E-value: 1.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    508 SVMCVEGEAGSGKTTFLKRIAFLWASGCCPLLnrFQLVFYLSLSSITPDQ---GLANIICAQLLGAGGCISEVclSSIIQ 584
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRSGnarSLADLLFSQWPEPAAPVSEV--WAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064    585 QLQHQVLFLLDDYSGLASLPQA----------LHTLITKNYLSRTCLLIAVHTNKVRGIRPYLDTS--LEIKEFPFYNTV 652
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQldgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 26050064    653 SVLRKLFSHD 662
Cdd:pfam05729  157 QYVRKYFSDE 166
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
159-229 2.36e-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: 120.50  E-value: 2.36e-32
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26050064     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 6.96e-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: 118.92  E-value: 6.96e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064    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 8.42e-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: 115.83  E-value: 8.42e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  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 2.48e-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: 105.82  E-value: 2.48e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064    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 6.28e-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: 6.28e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064     277 NEELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:smart00238    1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
279-346 2.45e-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: 103.11  E-value: 2.45e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26050064  279 ELRMDTFKDWPHESPGAVEALVKAGLFYTGKRDIVQCFSCGGCMEKWAEGDNPIEDHTKFFPNCVFLQ 346
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
63-127 5.15e-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: 5.15e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26050064     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 1.41e-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: 92.33  E-value: 1.41e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26050064   61 AKRLKTFETYDKFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFSTRLRKLPIENHKKLRPECEFLLG 129
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVLL 69
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
432-810 2.10e-19

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 94.87  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  432 DLGQSEAQWLQEARSLSEQLRDTYTKATFRHMNLPEVYSSLGTDHLLSCDVSIISKHISQPvQGSLTIPEVFSNLNSVMC 511
Cdd:COG5635  106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLER-IESLKRLELLEAKKKRLL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  512 VEGEAGSGKTTFLKRIAFLWASGCCPLLNRfqLVFYLSLSSITPDQGLANIICAQLLGAGGCISEvclssIIQQL--QHQ 589
Cdd:COG5635  185 ILGEPGSGKTTLLRYLALELAERYLDAEDP--IPILIELRDLAEEASLEDLLAEALEKRGGEPED-----ALERLlrNGR 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  590 VLFLLDDY------SGLASLPQALHTLITKNYLSR---TCLLIAVHTNKVRGIRPY----LDTSlEIKEFpfyntvsvLR 656
Cdd:COG5635  258 LLLLLDGLdevpdeADRDEVLNQLRRFLERYPKARviiTSRPEGYDSSELEGFEVLelapLSDE-QIEEF--------LK 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  657 KLFSHDIMRVRKFINYFGFHEELQGIHKTPLFVAAVCtDWFKNPSDQPFQDVALFKAYMQYLsLKHKGAAKPLQATVSS- 735
Cdd:COG5635  329 KWFEATERKAERLLEALEENPELRELARNPLLLTLLA-LLLRERGELPDTRAELYEQFVELL-LERWDEQRGLTIYRELs 406
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  736 -------CGQLALTGLFSSCFEFNSDNLaeagvdeDEELTTCLMSKFTAQRL---------------RPVYRFLGPLFQE 793
Cdd:COG5635  407 reelrelLSELALAMQENGRTEFAREEL-------EEILREYLGRRKDAEALldelllrtgllvergEGRYSFAHRSFQE 479
                        410
                 ....*....|....*..
gi 26050064  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 1.17e-05

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: 49.28  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1106 RLELSRED-QELLLTLPALQSLEVSETNQLPD---QLFHNLHKFLGLKELCVRLD---GKPNVLSVLPREFPNLHHMEKL 1178
Cdd:cd00116    7 GELLKTERaTELLPKLLCLQVLRLEGNTLGEEaakALASALRPQPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLQEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1179 SIRTSTES-DLSKLVKLIQNSPNLHVFHL------------KC-----------------NFLSN--CEPLMTVLASCKK 1226
Cdd:cd00116   87 DLSDNALGpDGCGVLESLLRSSSLQELKLnnnglgdrglrlLAkglkdlppaleklvlgrNRLEGasCEALAKALRANRD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1227 LREIEFSG---RCFEAMTFVNILPNFVFLKILNLRDQQFPDKETSeKFGQALGSLRNLEKLFVptgdgihqvaklivRQC 1303
Cdd:cd00116  167 LKELNLANngiGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGAS-ALAETLASLKSLEVLNL--------------GDN 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1304 LqlpclrvlvfaetLDDDSVLEIAKgATRGGFQKLENLDLTLNHkITEEGYRNFFQVLDNLPNLKNLDIS 1373
Cdd:cd00116  232 N-------------LTDAGAAALAS-ALLSPNISLLTLSLSCND-ITDDGAKDLAEVLAEKESLLELDLR 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1091-1347 1.67e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1091 ALELSKASVTKCSMSRLELSREDQELLLTLPALQSLEVSETNQLPDQLFHNLHKFLGLKEL--CVRLDGKPNVLSVLPRE 1168
Cdd:COG4886   52 LLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLtnLESLDLSGNQLTDLPEE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1169 FPNLHHMEKLSIRtstESDLSKLVKLIQNSPNLHVFHLKCNFLSNcepLMTVLASCKKLREIEFSGRCFEAMTFVniLPN 1248
Cdd:COG4886  132 LANLTNLKELDLS---NNQLTDLPEPLGNLTNLKSLDLSNNQLTD---LPEELGNLTNLKELDLSNNQITDLPEP--LGN 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1249 FVFLKILNLRDQQFpdketsEKFGQALGSLRNLEKLFVpTGDGIHQVAKLivrqcLQLPCLRVLVFAETldddsvlEIAK 1328
Cdd:COG4886  204 LTNLEELDLSGNQL------TDLPEPLANLTNLETLDL-SNNQLTDLPEL-----GNLTNLEELDLSNN-------QLTD 264
                        250
                 ....*....|....*....
gi 26050064 1329 GATRGGFQKLENLDLTLNH 1347
Cdd:COG4886  265 LPPLANLTNLKTLDLSNNQ 283
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
489-611 5.47e-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: 42.31  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064  489 ISQPVQGSLTIPEVFSNLNSVMCVEGEAGSGKTTFLKRIafLWASGCC------PLLNRFQLVFYLSLSSITpDQGLANI 562
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKArlisflPKFSRNKLIFIDQLQFLI-DVGLGYL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26050064  563 ICAQLLG--AGGCISEVCLSSIIQQLQHQVLFLLDDYS-GLAslPQALHTLI 611
Cdd:cd03238   80 TLGQKLStlSGGELQRVKLASELFSEPPGTLFILDEPStGLH--QQDINQLL 129
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1117-1371 1.22e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1117 LLTLPALQSLEVSEtNQLPDqLFHNLHKFLGLKELcvRLDGkpNVLSVLPREFPNLHHMEKLSIRTSTESDLSKLVKLiq 1196
Cdd:COG4886  178 LGNLTNLKELDLSN-NQITD-LPEPLGNLTNLEEL--DLSG--NQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNL-- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1197 nsPNLHVFHLKCNFLSNceplMTVLASCKKLREIEFSGrcfeamtfvNILPNFVFLKILNLRDQQFPDKETSEKFGQALG 1276
Cdd:COG4886  250 --TNLEELDLSNNQLTD----LPPLANLTNLKTLDLSN---------NQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1277 SLRNLEKLFVPTGDGIHQVAKLIVRQCLQLPCLRVLVFAETLDDDSVLEIAKGATRGGFQKLENLDLTLNHKITEEGYRN 1356
Cdd:COG4886  315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
                        250
                 ....*....|....*
gi 26050064 1357 FFQVLDNLPNLKNLD 1371
Cdd:COG4886  395 TTTAGVLLLTLALLD 409
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
1116-1235 1.47e-03

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: 41.93  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1116 LLLTLPALQSLEVSETNQLPDQLFHNLHKfLGLKElCVRLDGKPNVLSvlprefpNLHHMEKLSIRTSTESDLSKLVKLI 1195
Cdd:cd09293    4 LLFILHKLGQITQSNISQLLRILHSGLEW-LELYM-CPISDPPLDQLS-------NCNKLKKLILPGSKLIDDEGLIALA 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 26050064 1196 QNSPNLHVFHLK-CNFLSNcEPLMTVLASCKKLREIEFsGR 1235
Cdd:cd09293   75 QSCPNLQVLDLRaCENITD-SGIVALATNCPKLQTINL-GR 113
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1158-1409 4.32e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1158 KPNVLSVLPREFPNLHHMEKLSIRTSTESDLSKLVKLIQNSPNLHVFHLKCNFLSNCEPLmtvlASCKKLREIEFSGRCF 1237
Cdd:COG4886   50 TLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL----SNLTNLESLDLSGNQL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1238 EAMTfvNILPNFVFLKILNLRDQQFpdketsEKFGQALGSLRNLEKLFVpTGDGIHQVAKLIvrqcLQLPCLRVLvfaeT 1317
Cdd:COG4886  126 TDLP--EELANLTNLKELDLSNNQL------TDLPEPLGNLTNLKSLDL-SNNQLTDLPEEL----GNLTNLKEL----D 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26050064 1318 LDDDSVLEIakGATRGGFQKLENLDLTLNhKITEegyrnFFQVLDNLPNLKNLDISrhipeciqiqaitvkalGQCVSRL 1397
Cdd:COG4886  189 LSNNQITDL--PEPLGNLTNLEELDLSGN-QLTD-----LPEPLANLTNLETLDLS-----------------NNQLTDL 243
                        250
                 ....*....|..
gi 26050064 1398 PSLTRLGMLSWL 1409
Cdd:COG4886  244 PELGNLTNLEEL 255
 
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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