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Conserved domains on  [gi|1046903454|ref|XP_017451775|]
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peptidylglycine alpha-amidating monooxygenase isoform X1 [Rattus norvegicus]

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 ...
 503-810 4.96e-148

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: 440.93  E-value: 4.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 503 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 583 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 663 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903454 742 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 201-347 2.53e-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: 213.65  E-value: 2.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 270 LP--QAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakYALSFMTCTKNVAPDMFRTIP 347
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 64-173 9.05e-27

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: 106.18  E-value: 9.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046903454 137 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 173
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 ...
 503-810 4.96e-148

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: 440.93  E-value: 4.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 503 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 583 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 663 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903454 742 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 201-347 2.53e-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: 213.65  E-value: 2.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 270 LP--QAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakYALSFMTCTKNVAPDMFRTIP 347
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 64-173 9.05e-27

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: 106.18  E-value: 9.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046903454 137 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 173
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
560-810 5.37e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 76.21  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 560 DTILVIDPNNAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNhfcqPTDV 639
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 640 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFVTqwgeessGSSPRPGQFsvPHSLALVPhLDQLCVADRENGRIQCFKTDT 718
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEVTE-------FPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 719 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 798
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246

                         250
                  ....*....|..
gi 1046903454 799 GDAHTNTVWKFT 810
Cdd:COG4257   247 AESGANRIVRFD 258
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 646-810 8.35e-04

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: 42.70  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 646 GAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREI 725
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 726 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 802
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205


                  ....*...
gi 1046903454 803 TNTVWKFT 810
Cdd:pfam17170 206 SPTVYKIM 213
 
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 ...
 503-810 4.96e-148

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: 440.93  E-value: 4.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 503 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 583 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 663 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903454 742 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
Cdd:cd14958   229 GLLYVVDGPPRLNRSLPVRGFVIRIGKGLILGRFGPGGkapGQFQNPHDIAVDSGGDIYVGELGPNRVQKFV 300
Cu2_monoox_C pfam03712
Copper type II ascorbate-dependent monooxygenase, C-terminal domain; The N and C-terminal ...
 201-347 2.53e-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: 213.65  E-value: 2.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 270 LP--QAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakYALSFMTCTKNVAPDMFRTIP 347
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 ...
 518-809 5.55e-45

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: 163.26  E-value: 5.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 518 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPNNAEILQ--SSGKNL--FYLPHGLSIDTDG 593
Cdd:cd05819    11 QGIAVDSSGNIYVADTGNN------------------------RIQVFDPDGNFITSfgSFGSGDgqFNEPAGVAVDSDG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 594 NYWVTDVALHQVFKLDPHSKEgpLLILGRSmqpGSDQNHFCQPTDVAVEPStGAVFVSDgYCNSRIVQFSPSGKFVTQWG 673
Cdd:cd05819    67 NLYVADTGNHRIQKFDPDGNF--LASFGGS---GDGDGEFNGPRGIAVDSS-GNIYVAD-TGNHRIQKFDPDGEFLTTFG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 674 EESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTkEFVREIKHASFGRNVFaiSYIPGFLFAVNGKPYF 753
Cdd:cd05819   140 SGGSG----PGQFNGPTGVAVDSD-GNIYVADTGNHRIQVFDPDG-NFLTTFGSTGTGPGQF--NYPTGIAVDSDGNIYV 211

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903454 754 GDQEPVQGFVMNFSSGEIID--VFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKF 809
Cdd:cd05819   212 ADSGNNRVQVFDPDGAGFGGngNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 64-173 9.05e-27

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: 106.18  E-value: 9.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046903454 137 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 173
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 576-810 2.42e-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: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDphSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 655
Cdd:cd14955   104 SGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFD--SSGTFITKWGSF---GSGDGQFNSPTGIAVD-SAGNVYVADTG- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 656 NSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDTkEFVreikhASFGrnvf 735
Cdd:cd14955   177 NNRIQKFTSTGTFLTKWGSEGSG----DGQFNAPYGIA-VDSAGNVYVADTGNNRIQKFDSSG-TFI-----TKWG---- 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903454 736 aiSYIPGflfavngkpyfgdqepvqgfvmnfsSGEiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
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) ...
 560-809 1.39e-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: 104.67  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 560 DTILVIDPNNAEI----LQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKegpllILGRSMQPGSDQNHFCQ 635
Cdd:cd14956    81 DRIQVFTLTGELQtiggSSGSGPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGS-----FLRQWGGTGIEPGSFNY 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 636 PTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPhLDQLCVADRENGRIQCFK 715
Cdd:cd14956   156 PRGVAVDPD-GTLYVADTY-NDRIQVFDNDGAFLRKWGGRGTG----PGQFNYPYGIAIDP-DGNVFVADFGNNRIQKFT 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 716 TDtkefvreikhasfGRnvfaisyipgFLFAVNGKPyfgdQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGT 795
Cdd:cd14956   229 AD-------------GT----------FLTSWGSPG----TGPGQ---------------------FKNPWGVVVDADGT 260

                         250
                  ....*....|....
gi 1046903454 796 VYIGDAHTNTVWKF 809
Cdd:cd14956   261 VYVADSNNNRVQRF 274
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 516-714 7.82e-22

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: 96.49  E-value: 7.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 516 QVSGVALDSKNNLvifhrgdHVWD-GNS----FDSKFVY------------QQRGLGPIEEDT---ILVIDPNNAEI--L 573
Cdd:cd14955    64 SPTGIAVDSDGNV-------YVADtGNHriqkFDSTGTFltkwgssgsgdgQFNSPSGIAVDSagnVYVTDSGNNRIqkF 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 574 QSSGKNL------------FYLPHGLSIDTDGNYWVTDVALHQVFKLDphSKEGPLLILGRsmqPGSDQNHFCQPTDVAV 641
Cdd:cd14955   137 DSSGTFItkwgsfgsgdgqFNSPTGIAVDSAGNVYVADTGNNRIQKFT--STGTFLTKWGS---EGSGDGQFNAPYGIAV 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903454 642 EpSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 714
Cdd:cd14955   212 D-SAGNVYVADTG-NNRIQKFDSSGTFITKWGSEGSG----DGQFNSPSGIA-VDSAGNVYVADSGNNRIQKF 277
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 576-812 1.78e-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: 95.72  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHskeGPLLILGRSmqPGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 655
Cdd:cd14955    10 SGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDST---GTFLTKWGS--SGSGDGQFYSPTGIAVD-SDGNVYVADTG- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 656 NSRIVQFSPSGKFVTQWGEESSGSsprpGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDtkefvreikhasfGrnvf 735
Cdd:cd14955    83 NHRIQKFDSTGTFLTKWGSSGSGD----GQFNSPSGIA-VDSAGNVYVTDSGNNRIQKFDSS-------------G---- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903454 736 aisyipgflfavngkpyfgdqepvqGFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 812
Cdd:cd14955   141 -------------------------TFITKWGSFGSGD------GQFNSPTGIAVDSAGNVYVADTGNNRIQKFTST 186
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 562-732 3.82e-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: 82.63  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 562 ILVIDPNNAE--ILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPhsKEGPLLILGRSMQpgsdqnhFCQPTDV 639
Cdd:cd14962    35 VFVFDLPNGKvfVIGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDR--DGKFLRAIGAGAL-------FKRPTGI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 640 AVEPSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTK 719
Cdd:cd14962   106 AVDPAGKRLYVVDTL-AHKVKVFDLDGRLLFDIGKRGSG----PGEFNLPTDLAVDRD-GNLYVTDTMNFRVQIFDADGK 179

                         170
                  ....*....|...
gi 1046903454 720 eFVReikhaSFGR 732
Cdd:cd14962   180 -FLR-----SFGE 186
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 514-714 1.16e-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: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 81.17  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 514 PGQ---VSGVALDSKNNLVI----FHRGDHVwdgnSFDSKFVYQ--QRGLGPIEedtilvidpnnaeilqssgknlFYLP 584
Cdd:cd14956   103 PGQfnaPRGVAVDADGNLYVadfgNQRIQKF----DPDGSFLRQwgGTGIEPGS----------------------FNYP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 585 HGLSIDTDGNYWVTDVALH--QVFKLDphskeGPLLI-LGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQ 661
Cdd:cd14956   157 RGVAVDPDGTLYVADTYNDriQVFDND-----GAFLRkWG---GRGTGPGQFNYPYGIAIDPD-GNVFVADFG-NNRIQK 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046903454 662 FSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 714
Cdd:cd14956   227 FTADGTFLTSWGSPGTG----PGQFKNPWGVV-VDADGTVYVADSNNNRVQRF 274
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 576-800 3.34e-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: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNLFYLPHGLSIDTDGNYWVTDVA--LHQVFkldphSKEGPLLilgRSMQPGSDQNHFCQPTDVAVepSTGAVFVSD- 652
Cdd:cd14963    50 TGPGEFKYPYGIAVDSDGNIYVADLYngRIQVF-----DPDGKFL---KYFPEKKDRVKLISPAGLAI--DDGKLYVSDv 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 653 GYcnSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGR 732
Cdd:cd14963   120 KK--HKVIVFDLEGKLLLEFGKPGSE----PGELSYPNGIAVDED-GNIYVADSGNGRIQVFDKNGK-FIKELNGSPDGK 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903454 733 NVFA----ISYIP-GFLFAVN---GKPYFGDQEPVQGFVMNfSSGEIIDVFKpvrkhfdMPHDIVASEDGTVYIGD 800
Cdd:cd14963   192 SGFVnprgIAVDPdGNLYVVDnlsHRVYVFDEQGKELFTFG-GRGKDDGQFN-------LPNGLFIDDDGRLYVTD 259
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 504-714 7.71e-16

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: 79.13  E-value: 7.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 504 ELDWPgvyllpgqvSGVALDSKNNLVIFHRGDH---VWDGN-SFDSKFVYQQRGLGPI---------EEDTILVIDPNN- 569
Cdd:cd14954    69 QFDRP---------AGVAVNSRGRIIVADKDNHriqVFDLNgRFLLKFGERGTKNGQFnypwgvavdSEGRIYVSDTRNh 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 570 -AEILQSSGKNL------------FYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKegPLLILGrsmQPGSDQNHFCQP 636
Cdd:cd14954   140 rVQVFDSDGQFIrkfgfegagpgqLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQ--FLRFFG---SEGSGNGQFKRP 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903454 637 TDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCF 714
Cdd:cd14954   215 RGVAVDDE-GNIIVADSG-NHRVQVFSPDGEFLCSFGTEGNG----EGQFDRPSGVAVTPD-GRIVVVDRGNHRIQVF 285
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 575-810 8.87e-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: 78.85  E-value: 8.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 575 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFKldphSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 652
Cdd:cd14957    11 GSGNGQFNTPRGIAVDSAGNIYVADTGNNriQVFT----SSGVYSYSIGSG---GTGSGQFNSPYGIAVD-SNGNIYVAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 653 gYCNSRIVQFSPSGKFVTQWGeeSSGSSprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFkTDTKEFVREIKHASFGR 732
Cdd:cd14957    83 -TDNNRIQVFNSSGVYQYSIG--TGGSG--DGQFNGPYGIAVDSN-GNIYVADTGNHRIQVF-TSSGTFSYSIGSGGTGP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 733 NVFaiSYIPGFLFAVNGKPYFGDQ--EPVQGFVmnfSSGEIIDVF---KPVRKHFDMPHDIVASEDGTVYIGDAHTNTVW 807
Cdd:cd14957   156 GQF--NGPQGIAVDSDGNIYVADTgnHRIQVFT---SSGTFQYTFgssGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQ 230


                  ...
gi 1046903454 808 KFT 810
Cdd:cd14957   231 VFT 233
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 627-814 1.27e-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: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 78.10  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 627 GSDQNHFCQPTDVAVepSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADR 706
Cdd:cd14963     3 GPFGDPLNKPMGVAV--SDGRIYVADTN-NHRVQVFDYEGKFKKSFGGPGTG----PGEFKYPYGIAVDSD-GNIYVADL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 707 ENGRIQCFKTDTKeFVReikhaSFGRNVFAISYI-PGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRK--HFD 783
Cdd:cd14963    75 YNGRIQVFDPDGK-FLK-----YFPEKKDRVKLIsPAGLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEpgELS 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1046903454 784 MPHDIVASEDGTVYIGDAHTNTVWKFTLTEK 814
Cdd:cd14963   149 YPNGIAVDEDGNIYVADSGNGRIQVFDKNGK 179
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 518-714 2.36e-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: 77.69  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 518 SGVALDSKNNLvifhrgdHVWDGNS-----FDSKFVYQQ------RGLGPIEE---------DTILVIDPNNAEI--LQS 575
Cdd:cd14957    68 YGIAVDSNGNI-------YVADTDNnriqvFNSSGVYQYsigtggSGDGQFNGpygiavdsnGNIYVADTGNHRIqvFTS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNL------------FYLPHGLSIDTDGNYWVTDVALH--QVFkldphSKEGPLLilgRSM-QPGSDQNHFCQPTDVA 640
Cdd:cd14957   141 SGTFSysigsggtgpgqFNGPQGIAVDSDGNIYVADTGNHriQVF-----TSSGTFQ---YTFgSSGSGPGQFSDPYGIA 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903454 641 VEpSTGAVFVSDgYCNSRIVQFSPSGKFVTQWGeeSSGSSprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 714
Cdd:cd14957   213 VD-SDGNIYVAD-TGNHRIQVFTSSGAYQYSIG--TSGSG--NGQFNYPYGIA-VDNDGKIYVADSNNNRIQVF 279
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
560-810 5.37e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 76.21  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 560 DTILVIDPNNAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNhfcqPTDV 639
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 640 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFVTqwgeessGSSPRPGQFsvPHSLALVPhLDQLCVADRENGRIQCFKTDT 718
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEVTE-------FPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 719 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 798
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246

                         250
                  ....*....|..
gi 1046903454 799 GDAHTNTVWKFT 810
Cdd:COG4257   247 AESGANRIVRFD 258
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 581-812 9.94e-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: 75.40  E-value: 9.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 581 FYLPHGLSIDTDGNYWVTDVALH--QVFKLDPHSKegpllilGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDgYCNSR 658
Cdd:cd14956    12 FKDPRGIAVDADDNVYVADARNGriQVFDKDGTFL-------RRFGTTGDGPGQFGRPRGLAVDK-DGWLYVAD-YWGDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 659 IVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDqLCVADRENGRIQCFKTDTKeFVREIkhasfgrnvfais 738
Cdd:cd14956    83 IQVFTLTGELQTIGGSSGSG----PGQFNAPRGVAVDADGN-LYVADFGNQRIQKFDPDGS-FLRQW------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903454 739 yipgflfavnGKPyfgDQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 812
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 ...
 575-806 3.79e-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: 73.84  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 575 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkldpHSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 652
Cdd:cd14957    58 GTGSGQFNSPYGIAVDSNGNIYVADTDNNriQVF----NSSGVYQYSIGTG---GSGDGQFNGPYGIAVD-SNGNIYVAD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 653 GYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFkTDTKEFVREIKHASFGR 732
Cdd:cd14957   130 TG-NHRIQVFTSSGTFSYSIGSGGTG----PGQFNGPQGIAVDSD-GNIYVADTGNHRIQVF-TSSGTFQYTFGSSGSGP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 733 NVFAISY-IpgflfAV--NGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDA 801
Cdd:cd14957   203 GQFSDPYgI-----AVdsDGNIYVADTgnHRIQvftssgAYQYSIGTSGSGN------GQFNYPYGIAVDNDGKIYVADS 271


                  ....*
gi 1046903454 802 HTNTV 806
Cdd:cd14957   272 NNNRI 276
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 581-806 4.37e-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: 67.96  E-value: 4.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 581 FYLPHGLSIDTDGNYWVTDVALH--QVFKLDP--HSKEGpllilgrsmQPGSDQNHFCQPTDVAVEpSTGAVFVSDGYcN 656
Cdd:cd14954    23 LCRPWGVAVDKDGRIIVADRSNNrvQVFDPDGkfLRKFG---------SYGSRDGQFDRPAGVAVN-SRGRIIVADKD-N 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 657 SRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDTKeFVREI-------KHAS 729
Cdd:cd14954    92 HRIQVFDLNGRFLLKFGERGTK----NGQFNYPWGVA-VDSEGRIYVSDTRNHRVQVFDSDGQ-FIRKFgfegagpGQLD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 730 FGRNVfAIS-----YIPGF------LFAVNGKP--YFGDQEPVQGFvMNFSSGEIID----------------VFKP--- 777
Cdd:cd14954   166 SPRGV-AVNpdgniVVSDFnnhrlqVFDPDGQFlrFFGSEGSGNGQ-FKRPRGVAVDdegniivadsgnhrvqVFSPdge 243

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1046903454 778 -VRK---------HFDMPHDIVASEDGTVYIGDAHTNTV 806
Cdd:cd14954   244 fLCSfgtegngegQFDRPSGVAVTPDGRIVVVDRGNHRI 282
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
506-718 6.22e-12

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 66.64  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 506 DWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGpieeDTILVIDPNNAEILQS--SGKNlfyl 583
Cdd:COG3391    40 ASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGS----GRVSVIDLATGKVVATipVGGG---- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 584 PHGLSIDTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSdqnhfcQPTDVAVEPSTGAVFVSDGYCN--SRIV 660
Cdd:COG3391   112 PRGLAVDPDGGRlYVADSGNGRVSVIDTATGK-----VVATIPVGA------GPHGIAVDPDGKRLYVANSGSNtvSVIV 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903454 661 Q-FSP-SGKFVTQWGEESSgssprpgqfsvPHSLALVPHLDQLCVADRENG-------RIQCFKTDT 718
Cdd:COG3391   181 SvIDTaTGKVVATIPVGGG-----------PVGVAVSPDGRRLYVANRGSNtsnggsnTVSVIDLAT 236
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
584-809 2.05e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 65.43  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 584 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRsmqpgsdqnhFCQPTDVAVEPStGAVFVSDGYcNSRIVQFS 663
Cdd:COG4257    19 PRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGG----------GSGPHGIAVDPD-GNLWFTDNG-NNRIGRID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 664 P-SGKFVTQWGeessgssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKEfVREIKHASFGRNVFAISYIPg 742
Cdd:COG4257    87 PkTGEITTFAL---------PGGGSNPHGIAFDPD-GNLWFTDQGGNRIGRLDPATGE-VTEFPLPTGGAGPYGIAVDP- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903454 743 flfavNGKPYFGDQEPVQGFVMNFSSGEiIDVFKPVRKhFDMPHDIVASEDGTVYIGDAHTNTVWKF 809
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) ...
 577-714 2.99e-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: 64.92  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 577 GKNLFYLPHGLSIDTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNHFCQPTDVAVEPStGAVFVSDGYc 655
Cdd:cd14962    95 AGALFKRPTGIAVDPAGKRlYVVDTLAHKVKVFDLDGRL-----LFDIGKRGSGPGEFNLPTDLAVDRD-GNLYVTDTM- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 656 NSRIVQFSPSGKFVTQWGE-------------------------ESS------------------GSSPRPGQFSVPHSL 692
Cdd:cd14962   168 NFRVQIFDADGKFLRSFGErgdgpgsfarpkgiavdsegniyvvDAAfdnvqifnpegellltvgGPGSGPGEFYLPSGI 247

                         170       180
                  ....*....|....*....|..
gi 1046903454 693 AlVPHLDQLCVADRENGRIQCF 714
Cdd:cd14962   248 A-IDKDDRIYVVDQFNRRIQVF 268
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 581-806 1.42e-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: 63.70  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 581 FYLPHGLSIDTDGNYWVTDVALHQVFKLDPhskEGPLLILGRSMQPGSDQN------HFCQPTDVAVEPStGAVFVSDGY 654
Cdd:cd14953   131 FNYPTGVAVDAAGNLYVADTGNHRIRKITP---DGVVTTVAGTGGAGYAGDgpataaQFNNPTGVAVDAA-GNLYVADRG 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 655 cNSRIVQFSPSGKFVTQWGEESSGSSPRPG----QFSVPHSLAlVPHLDQLCVADRENGRIqcfktdtkefvREIKHAsf 730
Cdd:cd14953   207 -NHRIRKITPDGVVTTVAGTGTAGFSGDGGataaQLNNPTGVA-VDAAGNLYVADSGNHRI-----------RKITPA-- 271

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903454 731 GRnvfaISYipgflFAVNGKPYFGDQEPVqgfvmnfssgeiidvfKPVRkhFDMPHDIVASEDGTVYIGDAHTNTV 806
Cdd:cd14953   272 GV----VTT-----VAGGGAGFSGDGGPA----------------TSAQ--FNNPTGVAVDAAGNLYVADTGNNRI 320
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 562-715 2.71e-10

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: 62.36  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 562 ILVIDPNN--AEILQSSGKNLFYL-------PHGLSIDTDGNYWVTDVALHQVFKLDPHSKegpllILGRSMQPGSDQNH 632
Cdd:cd14960    77 IIIADYDNkwVSIFSPDGKFKSKIgagklmgPKGVAVDRNGHIIVVDNKACCVFIFQPNGK-----LVTRFGSRGNGDRQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 633 FCQPTDVAVEpSTGAVFVSDgYCNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQ 712
Cdd:cd14960   152 FAGPHFAAVN-NNNEIIVTD-FHNHSVKVFNAEGEFLFKFGSNGEG----NGQFNAPTGVAVDSN-GNIIVADWGNSRIQ 224


                  ...
gi 1046903454 713 CFK 715
Cdd:cd14960   225 VFD 227
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 505-714 4.82e-10

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: 61.54  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 505 LDWP-GVYLLPGQVSgVAlDSKNN-LVIFhrgdhvwdgnSFDSKFVYQ--QRGLGP--------IEEDT---ILVIDPNN 569
Cdd:cd14963     9 LNKPmGVAVSDGRIY-VA-DTNNHrVQVF----------DYEGKFKKSfgGPGTGPgefkypygIAVDSdgnIYVADLYN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 570 AEI--LQSSGKNLFYLPH-----------GLSIDtDGNYWVTDVALHQVFKLDPHSKEgpLLILGRsmqPGSDQNHFCQP 636
Cdd:cd14963    77 GRIqvFDPDGKFLKYFPEkkdrvklispaGLAID-DGKLYVSDVKKHKVIVFDLEGKL--LLEFGK---PGSEPGELSYP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 637 TDVAVEPStGAVFVSD-GycNSRIVQFSPSGKFVTQWGEESSGSS----PR----------------------------- 682
Cdd:cd14963   151 NGIAVDED-GNIYVADsG--NGRIQVFDKNGKFIKELNGSPDGKSgfvnPRgiavdpdgnlyvvdnlshrvyvfdeqgke 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1046903454 683 ----------PGQFSVPHSLALVPHlDQLCVADRENGRIQCF 714
Cdd:cd14963   228 lftfggrgkdDGQFNLPNGLFIDDD-GRLYVTDRENNRVAVY 268
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 506-718 9.44e-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: 60.75  E-value: 9.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 506 DWPGVYLLPgqvSGVALDSKNNLVIFHrgdhvwDGNS----FDSKFVYQQRgLGPIEEDT-------------------- 561
Cdd:cd14961     5 GWPGTLNNP---TGVAVTPTGRVVVAD------DGNKriqvFDSDGNCLQQ-FGPKGDAGqdirypldvavtpdghivvt 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 562 ------ILVIDPNnAEILQSSGKNlFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSmqpgsdQNHFCQ 635
Cdd:cd14961    75 dagdrsVKVFSFD-GRLKLFVRKS-FSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLGILKKGQKL------CSQLCR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 636 PTDVAVEPStGAVFVSD-------GYCNSRIVQFSPSGKFVTQWGeeSSGSSPRPGQFSVPHSLAlVPHLDQLCVADREN 708
Cdd:cd14961   147 PRFVAVSRL-GAVAVTEhlfangtRSSSTRVKVFSSGGQLLGQID--SFGLNLVFPSLICASGVA-FDSEGNVIVADTGS 222

                         250
                  ....*....|
gi 1046903454 709 GRIQCFKTDT 718
Cdd:cd14961   223 GAILCLGKPE 232
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
648-806 1.18e-07

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: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 648 VFVSDGYcNSRIVQFSP-SGKFVTQWgeeSSGSSPrpgqfsvpHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIK 726
Cdd:COG3391    82 LYVANSG-SGRVSVIDLaTGKVVATI---PVGGGP--------RGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 727 hasFGRNVFAISYIP--GFLFAVNgkpyFGDQEpVQGFV--MNFSSGEIIDVFKPvrkhFDMPHDIVASEDG-TVYIGDA 801
Cdd:COG3391   150 ---VGAGPHGIAVDPdgKRLYVAN----SGSNT-VSVIVsvIDTATGKVVATIPV----GGGPVGVAVSPDGrRLYVANR 217


                  ....*
gi 1046903454 802 HTNTV 806
Cdd:COG3391   218 GSNTS 222
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 584-711 2.08e-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: 52.98  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 584 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLilgrsmqPGSDQNhfcQPTDVAVEpSTGAVFVSDGYcNSRIVQFS 663
Cdd:cd14952    12 PGGVAVDAAGNVYVADSGNNRVLKLAAGSTTQTVL-------PFTGLY---QPQGVAVD-AAGTVYVTDFG-NNRVLKLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1046903454 664 PsgkfvtqwGEESSGSSPRPGQfSVPHSLAlVPHLDQLCVADRENGRI 711
Cdd:cd14952    80 A--------GSTTQTVLPFTGL-NDPTGVA-VDAAGNVYVADTGNNRV 117
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 581-810 5.55e-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: 52.53  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 581 FYLPHGLSIDTDGNYWVTDVALHQVFKLDPhskEGPLLILGRSMQPGSD-----QNHFCQPTDVAVEPStGAVFVSDGYc 655
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKITP---DGVVTTVAGTGTAGFAdgggaAAQFNTPSGVAVDAA-GNLYVADTG- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 656 NSRIVQFSPSGKFVTQWGEESSGSSPRPG----QFSVPHSLALVPHLDqLCVADRENGRIQcfKTDTKEFVReikhasfg 731
Cdd:cd14953    97 NHRIRKITPDGVVSTLAGTGTAGFSDDGGataaQFNYPTGVAVDAAGN-LYVADTGNHRIR--KITPDGVVT-------- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903454 732 rnVFAISYIPGFLFAVNGkpyfgdqepvqgfvmnfssgeiidvfkpVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
Cdd:cd14953   166 --TVAGTGGAGYAGDGPA----------------------------TAAQFNNPTGVAVDAAGNLYVADRGNHRIRKIT 214
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
 627-800 6.52e-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: 51.89  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 627 GSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSgsspRPGQFSVPHSLALVPHLDQLCVADR 706
Cdd:cd14959    15 GSGEGQFNSPSGFCLG-EDEDILVADTN-NHRIQVFDKEGEFKFQFGIPGK----RDGQLWYPNKVAVCRVTGRYVVTDR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 707 ENG--RIQCFkTDTKEFVREikhasfgrnvFAISYI--PGFLfAVNGKPYFGDQEPVQGFVMNFS-SGEIIDVFKpVRKH 781
Cdd:cd14959    89 GNPrhRMQIF-TKRGQFVRK----------FGARYLqhVRGL-TVDAAGHIIVVESKVMRVFIFDeSGNVLKWFD-CSKY 155

                         170
                  ....*....|....*....
gi 1046903454 782 FDMPHDIVASeDGTVYIGD 800
Cdd:cd14959   156 LEEPSDVAVN-DNEIYICD 173
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
590-749 7.07e-07

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 51.62  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 590 DTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDqnhfcqPTDVAVEPSTGAVFVSDGYcNSRIVQFSP-SGK 667
Cdd:COG3391    76 GADGRRlYVANSGSGRVSVIDLATGK-----VVATIPVGGG------PRGLAVDPDGGRLYVADSG-NGRVSVIDTaTGK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 668 FVTQWgeeSSGSSprpgqfsvPHSLALVPHLDQLCVADRENGRI----QCFKTDTKEFVREIkhaSFGRNVFAISYIP-- 741
Cdd:COG3391   144 VVATI---PVGAG--------PHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATI---PVGGGPVGVAVSPdg 209


                  ....*...
gi 1046903454 742 GFLFAVNG 749
Cdd:COG3391   210 RRLYVANR 217
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 584-661 1.21e-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: 50.67  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903454 584 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLilgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQ 661
Cdd:cd14952   180 PSGVAVDTAGNVYVTDHGNNRVLKLAAGSTTPTVL-------PFTGLNG---PLGVAVD-AAGNVYVAD-RGNDRVVK 245
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
699-809 1.51e-05

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 47.38  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 699 DQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVfAISYIPGFLFAVNGKPYFgdqepVQgfVMNFSSGEIIDVFKPv 778
Cdd:COG3391    80 RRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGL-AVDPDGGRLYVADSGNGR-----VS--VIDTATGKVVATIPV- 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1046903454 779 rkhFDMPHDIVASEDG-TVYIGDAHTNTVWKF 809
Cdd:COG3391   151 ---GAGPHGIAVDPDGkRLYVANSGSNTVSVI 179
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
 576-669 2.17e-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: 47.26  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkldphSKEGPLLilgrsMQ---PGSDQNHFCQPTDVAVEPSTGAVFV 650
Cdd:cd14959    16 SGEGQFNSPSGFCLGEDEDILVADTNNHriQVF-----DKEGEFK-----FQfgiPGKRDGQLWYPNKVAVCRVTGRYVV 85

                          90       100
                  ....*....|....*....|
gi 1046903454 651 SD-GYCNSRIVQFSPSGKFV 669
Cdd:cd14959    86 TDrGNPRHRMQIFTKRGQFV 105
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 584-711 7.82e-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: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 584 PHGLSIDTDGNYWVTDVALHQVFKLDPhskegpllilGRSMQ---PGSDQNHfcqPTDVAVEPStGAVFVSDGYcNSRIV 660
Cdd:cd14952    96 PTGVAVDAAGNVYVADTGNNRVLKLAA----------GSNTQtvlPFTGLSN---PDGVAVDGA-GNVYVTDTG-NNRVL 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046903454 661 QFsPSGkfvtqwgeessGSSPRPGQF---SVPHSLAlVPHLDQLCVADRENGRI 711
Cdd:cd14952   161 KL-AAG-----------STTQTVLPFtglNSPSGVA-VDTAGNVYVTDHGNNRV 201
MALA cd12811
Mala s 1 allergenic protein and similar proteins; This family includes the yeast Malassezia ...
 636-741 1.07e-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: 45.32  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 636 PTDVAVEPStGAVFVSDGYCNSrIVQFSPSGKFVTQWGEESSGSSPRPGqFSvphSLALVPHLDQLCVADRENGRIQCFK 715
Cdd:cd12811   123 FQDSAQDSD-GNSYVVGALPPA-IAKVSPDGKTVTPWFLEAPNGSTRPG-YT---GIAYIPEDNVLLASGGEPGQLTRFD 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046903454 716 TD----TKEFVReIKHASFGRNVFAIsYIP 741
Cdd:cd12811   197 LSsatpTPIPVK-ISGENFGGLDDGE-KLP 224
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 514-715 1.24e-04

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: 45.03  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 514 PGQV---SGVALDSKNNLVIFHRGDHvW------DGnSFDSKFvYQQRGLGPI-----EEDTILVIDpNNA---EILQSS 576
Cdd:cd14960    60 PGQLqrpTGVAVTLNGDIIIADYDNK-WvsifspDG-KFKSKI-GAGKLMGPKgvavdRNGHIIVVD-NKAccvFIFQPN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 577 GK------------NLFYLPHGLSIDTDGNYWVTDVALHQVfKLdpHSKEGPLLILGRSMQPGSDQnhFCQPTDVAVEpS 644
Cdd:cd14960   136 GKlvtrfgsrgngdRQFAGPHFAAVNNNNEIIVTDFHNHSV-KV--FNAEGEFLFKFGSNGEGNGQ--FNAPTGVAVD-S 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903454 645 TGAVFVSDgYCNSRIVQFSPSGKFvtqwgEESSGSSPRPgqFSVPHSLALVPHlDQLCVADRENgriQCFK 715
Cdd:cd14960   210 NGNIIVAD-WGNSRIQVFDSSGSF-----LSYINTSADP--LYGPQGLALTSD-GHVVVADSGN---HCFK 268
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 576-720 1.44e-04

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: 44.57  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 576 SGKNLFYLPHGLSIDTDGNYWVTD-----ValhQVFKLDphskeGPLLIlGRSMQpGSDQNHFCQPTDVAVEPStGAVFV 650
Cdd:cd14961     5 GWPGTLNNPTGVAVTPTGRVVVADdgnkrI---QVFDSD-----GNCLQ-QFGPK-GDAGQDIRYPLDVAVTPD-GHIVV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903454 651 SDGYCNSRIVqFSPSGK---FVTqwgeessgssprpGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKE 720
Cdd:cd14961    74 TDAGDRSVKV-FSFDGRlklFVR-------------KSFSLPWGVAVNPS-GEILVTDSEAGKLFVLTVDFKL 131
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 646-810 8.35e-04

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: 42.70  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 646 GAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREI 725
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903454 726 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 802
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205


                  ....*...
gi 1046903454 803 TNTVWKFT 810
Cdd:pfam17170 206 SPTVYKIM 213
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 686-714 1.15e-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: 37.00  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|....*....
gi 1046903454 686 FSVPHSLALVPhLDQLCVADRENGRIQCF 714
Cdd:pfam01436   1 FNRPHGVAVDS-NGDIYVADSENHRVQVF 28
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 782-809 3.40e-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: 35.84  E-value: 3.40e-03
                          10        20
                  ....*....|....*....|....*...
gi 1046903454 782 FDMPHDIVASEDGTVYIGDAHTNTVWKF 809
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
 
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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