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Conserved domains on  [gi|1720354138|ref|XP_030108037|]
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peptidyl-glycine alpha-amidating monooxygenase isoform X7 [Mus musculus]

Protein Classification

peptidyl-glycine alpha-amidating monooxygenase( domain architecture ID 10471209)

peptidyl-glycine alpha-amidating monooxygenase is a bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
397-704 9.30e-149

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


:

Pssm-ID: 271328 [Multi-domain]  Cd Length: 300  Bit Score: 439.78  E-value: 9.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 397 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 476
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 477 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 556
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 557 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 635
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 636 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
200-346 3.00e-64

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


:

Pssm-ID: 461021  Cd Length: 157  Bit Score: 212.50  E-value: 3.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.49e-26

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


:

Pssm-ID: 460053  Cd Length: 130  Bit Score: 105.41  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354138 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
 
Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
397-704 9.30e-149

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271328 [Multi-domain]  Cd Length: 300  Bit Score: 439.78  E-value: 9.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 397 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 476
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 477 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 556
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 557 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 635
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 636 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
200-346 3.00e-64

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 461021  Cd Length: 157  Bit Score: 212.50  E-value: 3.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.49e-26

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 460053  Cd Length: 130  Bit Score: 105.41  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354138 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
454-704 1.67e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 71.59  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 454 DTILVIDPNKAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNhfcqPTDV 533
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 534 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFitqwgeeSSGSSPKPGQFsvPHSLALVPhLNQLCVADRENGRIQCFKTDT 612
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEV-------TEFPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 613 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 692
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246
                         250
                  ....*....|..
gi 1720354138 693 GDAHTNTVWKFT 704
Cdd:COG4257   247 AESGANRIVRFD 258
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
540-749 1.34e-05

6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important.


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 540 GAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREI 619
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 620 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 696
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354138 697 TNTVWKftLTESRLEVEHrSVKKAGIEVPEIkeaeaVVEPKVKNKPTSSELQK 749
Cdd:pfam17170 206 SPTVYK--IMDGELKPAY-EFDFGGKKNPSI-----DFLKKIETKGNEEFMYD 250
 
Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
397-704 9.30e-149

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271328 [Multi-domain]  Cd Length: 300  Bit Score: 439.78  E-value: 9.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 397 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 476
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 477 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 556
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 557 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 635
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 636 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
200-346 3.00e-64

Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 461021  Cd Length: 157  Bit Score: 212.50  E-value: 3.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
412-703 2.15e-43

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 158.64  E-value: 2.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 412 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPNKAEILQ--SSGKNL--FYLPHGLSIDTDG 487
Cdd:cd05819    11 QGIAVDSSGNIYVADTGNN------------------------RIQVFDPDGNFITSfgSFGSGDgqFNEPAGVAVDSDG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 488 NYWVTDVALHQVFKLeprSKEG-PLLVLGRSmqpGSDQNHFCQPTDVAVEPStGAVFVSDgYCNSRIVQFSPSGKFITQW 566
Cdd:cd05819    67 NLYVADTGNHRIQKF---DPDGnFLASFGGS---GDGDGEFNGPRGIAVDSS-GNIYVAD-TGNHRIQKFDPDGEFLTTF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 567 GEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTkEFVREIKHASFGRNVFaiSYIPGFLFAVNGKPY 646
Cdd:cd05819   139 GSGGSG----PGQFNGPTGVAVDSD-GNIYVADTGNHRIQVFDPDG-NFLTTFGSTGTGPGQF--NYPTGIAVDSDGNIY 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354138 647 FGDQEPVQGFVMNFSSGEIID--VFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKF 703
Cdd:cd05819   211 VADSGNNRVQVFDPDGAGFGGngNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.49e-26

Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.


Pssm-ID: 460053  Cd Length: 130  Bit Score: 105.41  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354138 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
470-704 1.79e-25

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 106.89  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 470 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEprSKEGPLLVLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 549
Cdd:cd14955   104 SGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFD--SSGTFITKWGSF---GSGDGQFNSPTGIAVD-SAGNVYVADTG- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 550 NSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDTkEFVreikhASFGrnvf 629
Cdd:cd14955   177 NNRIQKFTSTGTFLTKWGSEGSG----DGQFNAPYGIA-VDSAGNVYVADTGNNRIQKFDSSG-TFI-----TKWG---- 241
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354138 630 aiSYIPGflfavngkpyfgdqepvqgfvmnfsSGEiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14955   242 --SEGSG-------------------------DGQ-----------FNSPSGIAVDSAGNVYVADSGNNRIQKFA 278
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
454-703 8.20e-24

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 101.98  E-value: 8.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 454 DTILVIDPNKAEI----LQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKegpllVLGRSMQPGSDQNHFCQ 529
Cdd:cd14956    81 DRIQVFTLTGELQtiggSSGSGPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGS-----FLRQWGGTGIEPGSFNY 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 530 PTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPhLNQLCVADRENGRIQCFK 609
Cdd:cd14956   156 PRGVAVDPD-GTLYVADTY-NDRIQVFDNDGAFLRKWGGRGTG----PGQFNYPYGIAIDP-DGNVFVADFGNNRIQKFT 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 610 TDtkefvreikhasfGRnvfaisyipgFLFAVNGKPyfgdQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGT 689
Cdd:cd14956   229 AD-------------GT----------FLTSWGSPG----TGPGQ---------------------FKNPWGVVVDADGT 260
                         250
                  ....*....|....
gi 1720354138 690 VYIGDAHTNTVWKF 703
Cdd:cd14956   261 VYVADSNNNRVQRF 274
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
412-608 1.88e-21

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 95.34  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 412 SGVALDSKNNLvifhrgdHVWDGNS-----FDS--KFVYQQRGLGpieedtilvidpnkaeilqsSGKNLFYLPHGLSID 484
Cdd:cd14955   113 SGIAVDSAGNV-------YVTDSGNnriqkFDSsgTFITKWGSFG--------------------SGDGQFNSPTGIAVD 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 485 TDGNYWVTDVALHQVFKLEPRSkeGPLLVLGRsmqPGSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFIT 564
Cdd:cd14955   166 SAGNVYVADTGNNRIQKFTSTG--TFLTKWGS---EGSGDGQFNAPYGIAVD-SAGNVYVADTG-NNRIQKFDSSGTFIT 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720354138 565 QWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 608
Cdd:cd14955   239 KWGSEGSG----DGQFNSPSGIA-VDSAGNVYVADSGNNRIQKF 277
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
521-706 5.52e-21

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 93.80  E-value: 5.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 521 GSDQNHFCQPTDVAVEpSTGAVFVSDgYCNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADR 600
Cdd:cd14955     9 GSGDGQFNSPSGIAVD-SAGNVYVAD-TGNNRIQKFDSTGTFLTKWGSSGSG----DGQFYSPTGIAVDSDGN-VYVADT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 601 ENGRIQCFkTDTKEFVReiKHASFGRNVFAISYIPGFLFAVNGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpv 672
Cdd:cd14955    82 GNHRIQKF-DSTGTFLT--KWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSgnNRIQkfdssgTFITKWGSFGSGD----- 153
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720354138 673 rKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 706
Cdd:cd14955   154 -GQFNSPTGIAVDSAGNVYVADTGNNRIQKFTST 186
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
408-608 1.88e-18

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 86.18  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 408 PGQ---VSGVALDSKNNLVI----FHRGDHVwdgnSFDSKFVYQ--QRGLGPIEedtilvidpnkaeilqssgknlFYLP 478
Cdd:cd14956   103 PGQfnaPRGVAVDADGNLYVadfgNQRIQKF----DPDGSFLRQwgGTGIEPGS----------------------FNYP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 479 HGLSIDTDGNYWVTDVALH--QVFKLEPRskegPLLVLGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQF 556
Cdd:cd14956   157 RGVAVDPDGTLYVADTYNDriQVFDNDGA----FLRKWG---GRGTGPGQFNYPYGIAIDPD-GNVFVADFG-NNRIQKF 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 557 SPSGKFITQWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 608
Cdd:cd14956   228 TADGTFLTSWGSPGTG----PGQFKNPWGVV-VDADGTVYVADSNNNRVQRF 274
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
470-694 4.92e-17

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 81.95  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 470 SGKNLFYLPHGLSIDTDGNYWVTDVA--LHQVFkleprSKEGPLLvlgRSMQPGSDQNHFCQPTDVAVepSTGAVFVSD- 546
Cdd:cd14963    50 TGPGEFKYPYGIAVDSDGNIYVADLYngRIQVF-----DPDGKFL---KYFPEKKDRVKLISPAGLAI--DDGKLYVSDv 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 547 GYcnSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGR 626
Cdd:cd14963   120 KK--HKVIVFDLEGKLLLEFGKPGSE----PGELSYPNGIAVDED-GNIYVADSGNGRIQVFDKNGK-FIKELNGSPDGK 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354138 627 NVFA----ISYIP-GFLFAVN---GKPYFGDQEPVQGFVMNfSSGEIIDVFKpvrkhfdMPHDIVASEDGTVYIGD 694
Cdd:cd14963   192 SGFVnprgIAVDPdGNLYVVDnlsHRVYVFDEQGKELFTFG-GRGKDDGQFN-------LPNGLFIDDDGRLYVTD 259
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
471-626 6.52e-17

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 81.86  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 471 GKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPrsKEGPLLVLGRSMQpgsdqnhFCQPTDVAVEPSTGAVFVSDGYcN 550
Cdd:cd14962    52 GPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDR--DGKFLRAIGAGAL-------FKRPTGIAVDPAGKRLYVVDTL-A 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354138 551 SRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFKTDTKeFVReikhaSFGR 626
Cdd:cd14962   122 HKVKVFDLDGRLLFDIGKRGSG----PGEFNLPTDLAVDRDGN-LYVTDTMNFRVQIFDADGK-FLR-----SFGE 186
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
469-704 2.84e-16

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271327 [Multi-domain]  Cd Length: 280  Bit Score: 80.00  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 469 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLVLGRSmqPGSDQNHFCQPTDVAVEpSTGAVFVSD 546
Cdd:cd14957    11 GSGNGQFNTPRGIAVDSAGNIYVADTGNNriQVF-----TSSGVYSYSIGS--GGTGSGQFNSPYGIAVD-SNGNIYVAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 547 gYCNSRIVQFSPSGKFITQWGeeSSGSSpkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFkTDTKEFVREIKHASFGR 626
Cdd:cd14957    83 -TDNNRIQVFNSSGVYQYSIG--TGGSG--DGQFNGPYGIAVDSNGN-IYVADTGNHRIQVF-TSSGTFSYSIGSGGTGP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 627 NVFaiSYIPGFLFAVNGKPYFGDQ--EPVQGFVmnfSSGEIIDVF---KPVRKHFDMPHDIVASEDGTVYIGDAHTNTVW 701
Cdd:cd14957   156 GQF--NGPQGIAVDSDGNIYVADTgnHRIQVFT---SSGTFQYTFgssGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQ 230

                  ...
gi 1720354138 702 KFT 704
Cdd:cd14957   231 VFT 233
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
521-725 2.85e-16

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 79.64  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 521 GSDQNHFCQPTDVAVepSTGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADR 600
Cdd:cd14963     3 GPFGDPLNKPMGVAV--SDGRIYVADTN-NHRVQVFDYEGKFKKSFGGPGTG----PGEFKYPYGIAVDSD-GNIYVADL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 601 ENGRIQCFKTDTKeFVReikhaSFGRNVFAISYI-PGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRK--HFD 677
Cdd:cd14963    75 YNGRIQVFDPDGK-FLK-----YFPEKKDRVKLIsPAGLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEpgELS 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720354138 678 MPHDIVASEDGTVYIGDAHTNTVWKFTLTESRL-EVEHRSVKKAGIEVP 725
Cdd:cd14963   149 YPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIkELNGSPDGKSGFVNP 197
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
413-608 1.19e-15

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 78.36  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 413 GVALDSKNNLVIFHRGDH---VWDGN-SFDSKFVYQQRGLGPIEEdtilvidpnkaeilqssgknlfylPHGLSIDTDGN 488
Cdd:cd14954   122 GVAVDSEGRIYVSDTRNHrvqVFDSDgQFIRKFGFEGAGPGQLDS------------------------PRGVAVNPDGN 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 489 YWVTDVALHQVFKLEPRSKegPLLVLGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGE 568
Cdd:cd14954   178 IVVSDFNNHRLQVFDPDGQ--FLRFFG---SEGSGNGQFKRPRGVAVDDE-GNIIVADSG-NHRVQVFSPDGEFLCSFGT 250
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720354138 569 ESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCF 608
Cdd:cd14954   251 EGNG----EGQFDRPSGVAVTPDGR-IVVVDRGNHRIQVF 285
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
475-706 1.82e-15

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 77.71  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 475 FYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDgYCNSR 552
Cdd:cd14956    12 FKDPRGIAVDADDNVYVADARNGriQVF-----DKDGTFL--RRFGTTGDGPGQFGRPRGLAVDK-DGWLYVAD-YWGDR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 553 IVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFKTDTKeFVREIkhasfgrnvfais 632
Cdd:cd14956    83 IQVFTLTGELQTIGGSSGSG----PGQFNAPRGVAVDADGN-LYVADFGNQRIQKFDPDGS-FLRQW------------- 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354138 633 yipgflfavnGKPyfgDQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 706
Cdd:cd14956   144 ----------GGT---GIEPGS---------------------FNYPRGVAVDPDGTLYVADTYNDRIQVFDND 183
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
469-608 3.01e-15

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271327 [Multi-domain]  Cd Length: 280  Bit Score: 76.92  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 469 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGpllVLGRSM-QPGSDQNHFCQPTDVAVEpSTGAVFVS 545
Cdd:cd14957   152 GTGPGQFNGPQGIAVDSDGNIYVADTGNHriQVF-----TSSG---TFQYTFgSSGSGPGQFSDPYGIAVD-SDGNIYVA 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354138 546 DgYCNSRIVQFSPSGKFITQWGeeSSGSSpkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 608
Cdd:cd14957   223 D-TGNHRIQVFTSSGAYQYSIG--TSGSG--NGQFNYPYGIA-VDNDGKIYVADSNNNRIQVF 279
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
469-700 8.42e-14

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271327 [Multi-domain]  Cd Length: 280  Bit Score: 72.68  E-value: 8.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 469 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFKleprSKEGPLLVLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 546
Cdd:cd14957    58 GTGSGQFNSPYGIAVDSNGNIYVADTDNNriQVFN----SSGVYQYSIGTG---GSGDGQFNGPYGIAVD-SNGNIYVAD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 547 GYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFkTDTKEFVREIKHASFGR 626
Cdd:cd14957   130 TG-NHRIQVFTSSGTFSYSIGSGGTG----PGQFNGPQGIAVDSDGN-IYVADTGNHRIQVF-TSSGTFQYTFGSSGSGP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 627 NVFAISY-IpgflfAV--NGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDA 695
Cdd:cd14957   203 GQFSDPYgI-----AVdsDGNIYVADTgnHRIQvftssgAYQYSIGTSGSGN------GQFNYPYGIAVDNDGKIYVADS 271

                  ....*
gi 1720354138 696 HTNTV 700
Cdd:cd14957   272 NNNRI 276
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
454-704 1.67e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 71.59  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 454 DTILVIDPNKAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNhfcqPTDV 533
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 534 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFitqwgeeSSGSSPKPGQFsvPHSLALVPhLNQLCVADRENGRIQCFKTDT 612
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEV-------TEFPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 613 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 692
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246
                         250
                  ....*....|..
gi 1720354138 693 GDAHTNTVWKFT 704
Cdd:COG4257   247 AESGANRIVRFD 258
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
475-700 8.52e-13

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 69.88  E-value: 8.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 475 FYLPHGLSIDTDGNYWVTDVALH--QVFKleprsKEGPLL-VLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYcNS 551
Cdd:cd14954    23 LCRPWGVAVDKDGRIIVADRSNNrvQVFD-----PDGKFLrKFGSY---GSRDGQFDRPAGVAVN-SRGRIIVADKD-NH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 552 RIVQFSPSGKFITQWGEESSgsspKPGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDTKeFVREI-------KHASF 624
Cdd:cd14954    93 RIQVFDLNGRFLLKFGERGT----KNGQFNYPWGVA-VDSEGRIYVSDTRNHRVQVFDSDGQ-FIRKFgfegagpGQLDS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 625 GRNVfAIS-----YIPGF------LFAVNGKP--YFGDQEPVQGFvMNFSSGEIID----------------VFKP---- 671
Cdd:cd14954   167 PRGV-AVNpdgniVVSDFnnhrlqVFDPDGQFlrFFGSEGSGNGQ-FKRPRGVAVDdegniivadsgnhrvqVFSPdgef 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720354138 672 VRK---------HFDMPHDIVASEDGTVYIGDAHTNTV 700
Cdd:cd14954   245 LCSfgtegngegQFDRPSGVAVTPDGRIVVVDRGNHRI 282
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
408-608 5.60e-12

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 67.19  E-value: 5.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 408 PGQV---SGVALDSKNNLVIFHRGDH---VWDGN-SFDSKFvyQQRGlgpieedtilvidpnkaeilQSSGKnlFYLPHG 480
Cdd:cd14954    67 DGQFdrpAGVAVNSRGRIIVADKDNHriqVFDLNgRFLLKF--GERG--------------------TKNGQ--FNYPWG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 481 LSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlgrsMQPGSDQN---HFCQPTDVAVEPsTGAVFVSDgYCNSRIVQ 555
Cdd:cd14954   123 VAVDSEGRIYVSDTRNHrvQVF-----DSDGQFI-----RKFGFEGAgpgQLDSPRGVAVNP-DGNIVVSD-FNNHRLQV 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354138 556 FSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLcVADRENGRIQCF 608
Cdd:cd14954   191 FDPDGQFLRFFGSEGSG----NGQFKRPRGVAVDDEGNII-VADSGNHRVQVF 238
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
478-703 1.45e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 65.81  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRsmqpgsdqnhFCQPTDVAVEPStGAVFVSDGYcNSRIVQFS 557
Cdd:COG4257    19 PRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGG----------GSGPHGIAVDPD-GNLWFTDNG-NNRIGRID 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 558 PSGKFITQWgeessgssPKPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKEfVREIKHASFGRNVFAISYIPgf 637
Cdd:COG4257    87 PKTGEITTF--------ALPGGGSNPHGIAFDPD-GNLWFTDQGGNRIGRLDPATGE-VTEFPLPTGGAGPYGIAVDP-- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354138 638 lfavNGKPYFGDQEPVQGFVMNFSSGEiIDVFKPVRKhFDMPHDIVASEDGTVYIGDAHTNTVWKF 703
Cdd:COG4257   155 ----DGNLWVTDFGANAIGRIDPDTGT-LTEYALPTP-GAGPRGLAVDPDGNLWVADTGSGRIGRF 214
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
456-608 4.25e-11

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 64.53  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 456 ILVIDPNKAEILQSSGKNLFYLPHGLSIDTDGNY-WVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNHFCQPTDVA 534
Cdd:cd14962    80 VFVFDRDGKFLRAIGAGALFKRPTGIAVDPAGKRlYVVDTLAHKVKVFDLDGRL-----LFDIGKRGSGPGEFNLPTDLA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 535 VEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGE-------------------------ESS------------------ 571
Cdd:cd14962   155 VDRD-GNLYVTDTM-NFRVQIFDADGKFLRSFGErgdgpgsfarpkgiavdsegniyvvDAAfdnvqifnpegellltvg 232
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720354138 572 GSSPKPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 608
Cdd:cd14962   233 GPGSGPGEFYLPSGIA-IDKDDRIYVVDQFNRRIQVF 268
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
401-612 2.11e-10

NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271331 [Multi-domain]  Cd Length: 273  Bit Score: 62.29  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 401 WPGVYLLPgqvSGVALDSKNNLVIFHrgdhvwDGNS----FDSKFVYQQRgLGPIEEDT--------------------- 455
Cdd:cd14961     6 WPGTLNNP---TGVAVTPTGRVVVAD------DGNKriqvFDSDGNCLQQ-FGPKGDAGqdirypldvavtpdghivvtd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 456 -----ILVIDPNKaEILQSSGKNlFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSmqpgsdQNHFCQP 530
Cdd:cd14961    76 agdrsVKVFSFDG-RLKLFVRKS-FSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLGILKKGQKL------CSQLCRP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 531 TDVAVEPStGAVFVSD-------GYCNSRIVQFSPSGKFITQWGeeSSGSSPKPGQFSVPHSLAlVPHLNQLCVADRENG 603
Cdd:cd14961   148 RFVAVSRL-GAVAVTEhlfangtRSSSTRVKVFSSGGQLLGQID--SFGLNLVFPSLICASGVA-FDSEGNVIVADTGSG 223

                  ....*....
gi 1720354138 604 RIQCFKTDT 612
Cdd:cd14961   224 AILCLGKPE 232
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
412-605 2.88e-10

Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 62.55  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 412 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPN-KAEILQSSGK----------NLFYLPHG 480
Cdd:cd14953    26 SGVAVDAAGNLYVADRGNH------------------------RIRKITPDgVVTTVAGTGTagfadgggaaAQFNTPSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 481 LSIDTDGNYWVTDVALHQVFKLEPrskEGPLLVL------GRSMQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIV 554
Cdd:cd14953    82 VAVDAAGNLYVADTGNHRIRKITP---DGVVSTLagtgtaGFSDDGGATAAQFNYPTGVAVDAA-GNLYVADTG-NHRIR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720354138 555 QFSPSGKFITQWGEESSGSSP-KPG---QFSVPHSLALVPHLNqLCVADRENGRI 605
Cdd:cd14953   157 KITPDGVVTTVAGTGGAGYAGdGPAtaaQFNNPTGVAVDAAGN-LYVADRGNHRI 210
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
478-609 2.21e-09

NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271330 [Multi-domain]  Cd Length: 274  Bit Score: 59.28  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKegpllVLGRSMQPGSDQNHFCQPTDVAVEpSTGAVFVSDgYCNSRIVQFS 557
Cdd:cd14960   108 PKGVAVDRNGHIIVVDNKACCVFIFQPNGK-----LVTRFGSRGNGDRQFAGPHFAAVN-NNNEIIVTD-FHNHSVKVFN 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 558 PSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFK 609
Cdd:cd14960   181 AEGEFLFKFGSNGEG----NGQFNAPTGVAVDSNGN-IIVADWGNSRIQVFD 227
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
402-608 3.48e-09

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 58.84  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 402 PGVYLLPgqvSGVALDSKNNLVI---FHRGDHVWD--GNsFDSKFVYQQRGLGP-------IEEDTILVID--PNKAEIL 467
Cdd:cd14963    52 PGEFKYP---YGIAVDSDGNIYVadlYNGRIQVFDpdGK-FLKYFPEKKDRVKLispaglaIDDGKLYVSDvkKHKVIVF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 468 QSSGKNLFYL------------PHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLL--VLGRSMQPGSdqnhFCQPT 531
Cdd:cd14963   128 DLEGKLLLEFgkpgsepgelsyPNGIAVDEDGNIYVADSGNGriQVF-----DKNGKFIkeLNGSPDGKSG----FVNPR 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354138 532 DVAVEPsTGAVFVSDGYCNsRIVQFSPSGKFITQWGeeSSGSSPkpGQFSVPHSLALVPHlNQLCVADRENGRIQCF 608
Cdd:cd14963   199 GIAVDP-DGNLYVVDNLSH-RVYVFDEQGKELFTFG--GRGKDD--GQFNLPNGLFIDDD-GRLYVTDRENNRVAVY 268
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
542-700 9.12e-08

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 53.93  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 542 VFVSDGYcNSRIVQFSP-SGKFITQWgeeSSGSSPkpgqfsvpHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREIK 620
Cdd:COG3391    82 LYVANSG-SGRVSVIDLaTGKVVATI---PVGGGP--------RGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 621 hasFGRNVFAISYIP--GFLFAVNgkpyFGDQEpVQGFV--MNFSSGEIIDVFKPvrkhFDMPHDIVASEDG-TVYIGDA 695
Cdd:COG3391   150 ---VGAGPHGIAVDPdgKRLYVAN----SGSNT-VSVIVsvIDTATGKVVATIPV----GGGPVGVAVSPDGrRLYVANR 217

                  ....*
gi 1720354138 696 HTNTV 700
Cdd:COG3391   218 GSNTS 222
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
474-605 1.82e-07

Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 54.07  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 474 LFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPllVLGRSMQPGSDQNH-----FCQPTDVAVEpSTGAVFVSDgY 548
Cdd:cd14953   185 QFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVTT--VAGTGTAGFSGDGGataaqLNNPTGVAVD-AAGNLYVAD-S 260
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354138 549 CNSRIVQFSPSGKFIT----QWGEESSGSSPKPGQFSVPHSLALVPHLNqLCVADRENGRI 605
Cdd:cd14953   261 GNHRIRKITPAGVVTTvaggGAGFSGDGGPATSAQFNNPTGVAVDAAGN-LYVADTGNNRI 320
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
475-704 1.95e-07

Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 53.69  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 475 FYLPHGLSIDTDGNYWVTDVALHQVFKLeprSKEGPLLVLGRSMQPGSD-----QNHFCQPTDVAVEPStGAVFVSDGYc 549
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKI---TPDGVVTTVAGTGTAGFAdgggaAAQFNTPSGVAVDAA-GNLYVADTG- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 550 NSRIVQFSPSGKFITQWGEESSGSSPKPG----QFSVPHSLALVPHLNqLCVADRENGRIQcfKTDTKEFVReikhasfg 625
Cdd:cd14953    97 NHRIRKITPDGVVSTLAGTGTAGFSDDGGataaQFNYPTGVAVDAAGN-LYVADTGNHRIR--KITPDGVVT-------- 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354138 626 rnVFAISYIPGFLFAVNGkpyfgdqepvqgfvmnfssgeiidvfkpVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14953   166 --TVAGTGGAGYAGDGPA----------------------------TAAQFNNPTGVAVDAAGNLYVADRGNHRIRKIT 214
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
478-605 3.19e-07

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 52.60  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLvlgrsmqPGSDQNhfcQPTDVAVEpSTGAVFVSDGYcNSRIVQFS 557
Cdd:cd14952    12 PGGVAVDAAGNVYVADSGNNRVLKLAAGSTTQTVL-------PFTGLY---QPQGVAVD-AAGTVYVTDFG-NNRVLKLA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 558 PsgkfitqwgeessGSS-PKPGQF---SVPHSLALVPHLNqLCVADRENGRI 605
Cdd:cd14952    80 A-------------GSTtQTVLPFtglNDPTGVAVDAAGN-VYVADTGNNRV 117
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
521-694 3.37e-07

NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271329 [Multi-domain]  Cd Length: 274  Bit Score: 52.66  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 521 GSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSgsspKPGQFSVPHSLALVPHLNQLCVADR 600
Cdd:cd14959    15 GSGEGQFNSPSGFCLG-EDEDILVADTN-NHRIQVFDKEGEFKFQFGIPGK----RDGQLWYPNKVAVCRVTGRYVVTDR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 601 ENG--RIQCFkTDTKEFVREikhasfgrnvFAISYI--PGFLfAVNGKPYFGDQEPVQGFVMNFS-SGEIIDVFKpVRKH 675
Cdd:cd14959    89 GNPrhRMQIF-TKRGQFVRK----------FGARYLqhVRGL-TVDAAGHIIVVESKVMRVFIFDeSGNVLKWFD-CSKY 155
                         170
                  ....*....|....*....
gi 1720354138 676 FDMPHDIVASeDGTVYIGD 694
Cdd:cd14959   156 LEEPSDVAVN-DNEIYICD 173
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
478-555 1.89e-06

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 50.28  E-value: 1.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpLLVLgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQ 555
Cdd:cd14952   180 PSGVAVDTAGNVYVTDHGNNRVLKLAAGSTT--PTVL-----PFTGLNG---PLGVAVD-AAGNVYVAD-RGNDRVVK 245
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
484-643 2.28e-06

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 49.69  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 484 DTDGNY-WVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDqnhfcqPTDVAVEPSTGAVFVSDGYcNSRIVQFSP-SGK 561
Cdd:COG3391    76 GADGRRlYVANSGSGRVSVIDLATGK-----VVATIPVGGG------PRGLAVDPDGGRLYVADSG-NGRVSVIDTaTGK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 562 FITQWgeeSSGSSpkpgqfsvPHSLALVPHLNQLCVADRENGRI----QCFKTDTKEFVREIkhaSFGRNVFAISYIP-- 635
Cdd:COG3391   144 VVATI---PVGAG--------PHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATI---PVGGGPVGVAVSPdg 209

                  ....*...
gi 1720354138 636 GFLFAVNG 643
Cdd:COG3391   210 RRLYVANR 217
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
593-703 7.86e-06

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.15  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 593 NQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVfAISYIPGFLFAVNGKPYFgdqepVQgfVMNFSSGEIIDVFKPv 672
Cdd:COG3391    80 RRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGL-AVDPDGGRLYVADSGNGR-----VS--VIDTATGKVVATIPV- 150
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720354138 673 rkhFDMPHDIVASEDG-TVYIGDAHTNTVWKF 703
Cdd:COG3391   151 ---GAGPHGIAVDPDGkRLYVANSGSNTVSVI 179
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
540-749 1.34e-05

6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important.


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 540 GAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREI 619
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 620 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 696
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354138 697 TNTVWKftLTESRLEVEHrSVKKAGIEVPEIkeaeaVVEPKVKNKPTSSELQK 749
Cdd:pfam17170 206 SPTVYK--IMDGELKPAY-EFDFGGKKNPSI-----DFLKKIETKGNEEFMYD 250
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
562-704 1.83e-05

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 47.57  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 562 FITQWGEESSGSspkpGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDtkefvreikhasfgrnvfaisyipGFLFAV 641
Cdd:cd14955     1 FVTQWGSYGSGD----GQFNSPSGIA-VDSAGNVYVADTGNNRIQKFDST------------------------GTFLTK 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354138 642 NGKPYFGDqepvqgfvmnfssGEiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFT 704
Cdd:cd14955    52 WGSSGSGD-------------GQ-----------FYSPTGIAVDSDGNVYVADTGNHRIQKFD 90
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
470-563 3.60e-05

NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271329 [Multi-domain]  Cd Length: 274  Bit Score: 46.49  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 470 SGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlgrsMQ---PGSDQNHFCQPTDVAVEPSTGAVFV 544
Cdd:cd14959    16 SGEGQFNSPSGFCLGEDEDILVADTNNHriQVF-----DKEGEFK-----FQfgiPGKRDGQLWYPNKVAVCRVTGRYVV 85
                          90       100
                  ....*....|....*....|
gi 1720354138 545 SD-GYCNSRIVQFSPSGKFI 563
Cdd:cd14959    86 TDrGNPRHRMQIFTKRGQFV 105
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
408-609 4.51e-05

NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271330 [Multi-domain]  Cd Length: 274  Bit Score: 46.18  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 408 PGQV---SGVALDSKNNLVIFHRGDHvW------DGnSFDSKFvYQQRGLGPI-----EEDTILVIDpNKA---EILQSS 470
Cdd:cd14960    60 PGQLqrpTGVAVTLNGDIIIADYDNK-WvsifspDG-KFKSKI-GAGKLMGPKgvavdRNGHIIVVD-NKAccvFIFQPN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 471 GK------------NLFYLPHGLSIDTDGNYWVTDVALHQVfKLepRSKEGPLLVLGRSMQPGSDQnhFCQPTDVAVEpS 538
Cdd:cd14960   136 GKlvtrfgsrgngdRQFAGPHFAAVNNNNEIIVTDFHNHSV-KV--FNAEGEFLFKFGSNGEGNGQ--FNAPTGVAVD-S 209
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354138 539 TGAVFVSDgYCNSRIVQFSPSGKFitqwgEESSGSSPKPgqFSVPHSLALVPHlNQLCVADRENgriQCFK 609
Cdd:cd14960   210 NGNIIVAD-WGNSRIQVFDSSGSF-----LSYINTSADP--LYGPQGLALTSD-GHVVVADSGN---HCFK 268
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
478-555 7.05e-05

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 45.28  E-value: 7.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSkeGPLLVLgrsmqPGSDQNHfcqPTDVAVEPStGAVFVSDGYcNSRIVQ 555
Cdd:cd14952    96 PTGVAVDAAGNVYVADTGNNRVLKLAAGS--NTQTVL-----PFTGLSN---PDGVAVDGA-GNVYVTDTG-NNRVLK 161
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
521-614 8.20e-05

NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271331 [Multi-domain]  Cd Length: 273  Bit Score: 45.34  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 521 GSDQNHFCQPTDVAVEPsTGAVFVSD-GycNSRIVQFSPSGKFITQWGEESSGSSPKP---------------------- 577
Cdd:cd14961     4 GGWPGTLNNPTGVAVTP-TGRVVVADdG--NKRIQVFDSDGNCLQQFGPKGDAGQDIRypldvavtpdghivvtdagdrs 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354138 578 ---------------GQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKE 614
Cdd:cd14961    81 vkvfsfdgrlklfvrKSFSLPWGVAVNPS-GEILVTDSEAGKLFVLTVDFKL 131
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
468-557 2.33e-04

Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271327 [Multi-domain]  Cd Length: 280  Bit Score: 43.79  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 468 QSSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGpllVLGRSM-QPGSDQNHFCQPTDVAVEpSTGAVFV 544
Cdd:cd14957   198 SGSGPGQFSDPYGIAVDSDGNIYVADTGNHriQVF-----TSSG---AYQYSIgTSGSGNGQFNYPYGIAVD-NDGKIYV 268
                          90
                  ....*....|...
gi 1720354138 545 SDGYcNSRIVQFS 557
Cdd:cd14957   269 ADSN-NNRIQVFN 280
MALA cd12811
Mala s 1 allergenic protein and similar proteins; This family includes the yeast Malassezia ...
530-635 4.58e-04

Mala s 1 allergenic protein and similar proteins; This family includes the yeast Malassezia sympodialis allergen Mala s 1 which is localized in the cell wall and exposed on the cell surface. It can elicit specific IgE and T-cell activity in patients with atopic eczema (AE), a chronic inflammatory disease. Mala s 1 does not show any significant sequence homology to characterized proteins. However, its structure is a beta-propeller which is a novel fold among allergens.


Pssm-ID: 411995 [Multi-domain]  Cd Length: 304  Bit Score: 43.39  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 530 PTDVAVEPStGAVFVSDGYCNSrIVQFSPSGKFITQWGEESSGSSPKPGqFSvphSLALVPHLNQLCVADRENGRIQCFK 609
Cdd:cd12811   123 FQDSAQDSD-GNSYVVGALPPA-IAKVSPDGKTVTPWFLEAPNGSTRPG-YT---GIAYIPEDNVLLASGGEPGQLTRFD 196
                          90       100       110
                  ....*....|....*....|....*....|
gi 1720354138 610 TD----TKEFVReIKHASFGRNVFAIsYIP 635
Cdd:cd12811   197 LSsatpTPIPVK-ISGENFGGLDDGE-KLP 224
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
580-608 7.56e-04

NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats.


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 37.38  E-value: 7.56e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720354138 580 FSVPHSLALVPhLNQLCVADRENGRIQCF 608
Cdd:pfam01436   1 FNRPHGVAVDS-NGDIYVADSENHRVQVF 28
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
478-558 1.77e-03

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 41.04  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 478 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLvlgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQFS 557
Cdd:cd14952   138 PDGVAVDGAGNVYVTDTGNNRVLKLAAGSTTQTVL-------PFTGLNS---PSGVAVD-TAGNVYVTD-HGNNRVLKLA 205

                  .
gi 1720354138 558 P 558
Cdd:cd14952   206 A 206
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
676-703 3.53e-03

NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats.


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 35.46  E-value: 3.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 1720354138 676 FDMPHDIVASEDGTVYIGDAHTNTVWKF 703
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
452-551 3.72e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.06  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354138 452 EEDTILVIDPNKAEILQS--SGKNlfylPHGLSIDTDGNY-WVTDVALHQ----VFKLEPRSKEgpllVLGRsMQPGSdq 524
Cdd:COG3391   130 GNGRVSVIDTATGKVVATipVGAG----PHGIAVDPDGKRlYVANSGSNTvsviVSVIDTATGK----VVAT-IPVGG-- 198
                          90       100
                  ....*....|....*....|....*..
gi 1720354138 525 nhfcQPTDVAVEPSTGAVFVSDGYCNS 551
Cdd:COG3391   199 ----GPVGVAVSPDGRRLYVANRGSNT 221
 
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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