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Conserved domains on  [gi|1958801070|ref|XP_038938973|]
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peptidylglycine alpha-amidating monooxygenase isoform X11 [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 ...
 398-705 4.69e-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: 440.55  E-value: 4.69e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 398 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 477
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 478 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 557
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 558 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 636
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801070 637 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 705
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 2.94e-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: 2.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 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 1.14e-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: 105.80  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958801070 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 ...
 398-705 4.69e-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: 440.55  E-value: 4.69e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 398 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 477
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 478 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 557
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 558 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 636
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801070 637 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 705
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 2.94e-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: 2.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 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 1.14e-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: 105.80  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958801070 137 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 173
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
455-705 5.26e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 76.21  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 455 DTILVIDPNNAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNhfcqPTDV 534
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 535 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFVTqwgeessGSSPRPGQFsvPHSLALVPhLDQLCVADRENGRIQCFKTDT 613
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEVTE-------FPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 614 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 693
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246

                         250
                  ....*....|..
gi 1958801070 694 GDAHTNTVWKFT 705
Cdd:COG4257   247 AESGANRIVRFD 258
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 541-705 7.89e-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: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 541 GAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREI 620
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 621 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 697
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205


                  ....*...
gi 1958801070 698 TNTVWKFT 705
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 ...
 398-705 4.69e-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: 440.55  E-value: 4.69e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 398 EELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNNaEILQSSGKNLFY 477
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 478 LPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 557
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 558 SPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 636
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801070 637 GFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVR---KHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 705
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 2.94e-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: 2.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 201 IAGMYLMMSV---DTVIPPGEKVVNADISCQYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQNPQ 269
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 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 ...
 413-704 1.07e-44

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: 162.10  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 413 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPNNAEILQ--SSGKNL--FYLPHGLSIDTDG 488
Cdd:cd05819    11 QGIAVDSSGNIYVADTGNN------------------------RIQVFDPDGNFITSfgSFGSGDgqFNEPAGVAVDSDG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 489 NYWVTDVALHQVFKLDPHSKEgpLLILGRSmqpGSDQNHFCQPTDVAVEPStGAVFVSDgYCNSRIVQFSPSGKFVTQWG 568
Cdd:cd05819    67 NLYVADTGNHRIQKFDPDGNF--LASFGGS---GDGDGEFNGPRGIAVDSS-GNIYVAD-TGNHRIQKFDPDGEFLTTFG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 569 EESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTkEFVREIKHASFGRNVFaiSYIPGFLFAVNGKPYF 648
Cdd:cd05819   140 SGGSG----PGQFNGPTGVAVDSD-GNIYVADTGNHRIQVFDPDG-NFLTTFGSTGTGPGQF--NYPTGIAVDSDGNIYV 211

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801070 649 GDQEPVQGFVMNFSSGEIID--VFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKF 704
Cdd:cd05819   212 ADSGNNRVQVFDPDGAGFGGngNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
 64-173 1.14e-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: 105.80  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070  64 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 136
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958801070 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 ...
 471-705 4.02e-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: 106.12  E-value: 4.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDphSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 550
Cdd:cd14955   104 SGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFD--SSGTFITKWGSF---GSGDGQFNSPTGIAVD-SAGNVYVADTG- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 551 NSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDTkEFVreikhASFGrnvf 630
Cdd:cd14955   177 NNRIQKFTSTGTFLTKWGSEGSG----DGQFNAPYGIA-VDSAGNVYVADTGNNRIQKFDSSG-TFI-----TKWG---- 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801070 631 aiSYIPGflfavngkpyfgdqepvqgfvmnfsSGEiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFT 705
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) ...
 455-704 1.32e-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: 104.29  E-value: 1.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 455 DTILVIDPNNAEI----LQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKegpllILGRSMQPGSDQNHFCQ 530
Cdd:cd14956    81 DRIQVFTLTGELQtiggSSGSGPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGS-----FLRQWGGTGIEPGSFNY 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 531 PTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPhLDQLCVADRENGRIQCFK 610
Cdd:cd14956   156 PRGVAVDPD-GTLYVADTY-NDRIQVFDNDGAFLRKWGGRGTG----PGQFNYPYGIAIDP-DGNVFVADFGNNRIQKFT 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 611 TDtkefvreikhasfGRnvfaisyipgFLFAVNGKPyfgdQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGT 690
Cdd:cd14956   229 AD-------------GT----------FLTSWGSPG----TGPGQ---------------------FKNPWGVVVDADGT 260

                         250
                  ....*....|....
gi 1958801070 691 VYIGDAHTNTVWKF 704
Cdd:cd14956   261 VYVADSNNNRVQRF 274
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 411-609 1.21e-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: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 411 QVSGVALDSKNNLvifhrgdHVWD-GNS----FDSKFVY------------QQRGLGPIEEDT---ILVIDPNNAEI--L 468
Cdd:cd14955    64 SPTGIAVDSDGNV-------YVADtGNHriqkFDSTGTFltkwgssgsgdgQFNSPSGIAVDSagnVYVTDSGNNRIqkF 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 469 QSSGKNL------------FYLPHGLSIDTDGNYWVTDVALHQVFKLDphSKEGPLLILGRsmqPGSDQNHFCQPTDVAV 536
Cdd:cd14955   137 DSSGTFItkwgsfgsgdgqFNSPTGIAVDSAGNVYVADTGNNRIQKFT--STGTFLTKWGS---EGSGDGQFNAPYGIAV 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801070 537 EpSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 609
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 ...
 471-707 2.76e-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: 94.95  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHskeGPLLILGRSmqPGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 550
Cdd:cd14955    10 SGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDST---GTFLTKWGS--SGSGDGQFYSPTGIAVD-SDGNVYVADTG- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 551 NSRIVQFSPSGKFVTQWGEESSGSsprpGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDtkefvreikhasfGrnvf 630
Cdd:cd14955    83 NHRIQKFDSTGTFLTKWGSSGSGD----GQFNSPSGIA-VDSAGNVYVTDSGNNRIQKFDSS-------------G---- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801070 631 aisyipgflfavngkpyfgdqepvqGFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 707
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) ...
 457-627 3.99e-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: 82.25  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 457 ILVIDPNNAE--ILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPhsKEGPLLILGRSMQpgsdqnhFCQPTDV 534
Cdd:cd14962    35 VFVFDLPNGKvfVIGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDR--DGKFLRAIGAGAL-------FKRPTGI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 535 AVEPSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTK 614
Cdd:cd14962   106 AVDPAGKRLYVVDTL-AHKVKVFDLDGRLLFDIGKRGSG----PGEFNLPTDLAVDRD-GNLYVTDTMNFRVQIFDADGK 179

                         170
                  ....*....|...
gi 1958801070 615 eFVReikhaSFGR 627
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) ...
 409-609 1.10e-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: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 409 PGQ---VSGVALDSKNNLVI----FHRGDHVwdgnSFDSKFVYQ--QRGLGPIEedtilvidpnnaeilqssgknlFYLP 479
Cdd:cd14956   103 PGQfnaPRGVAVDADGNLYVadfgNQRIQKF----DPDGSFLRQwgGTGIEPGS----------------------FNYP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 480 HGLSIDTDGNYWVTDVALH--QVFKLDphskeGPLLI-LGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQ 556
Cdd:cd14956   157 RGVAVDPDGTLYVADTYNDriQVFDND-----GAFLRkWG---GRGTGPGQFNYPYGIAIDPD-GNVFVADFG-NNRIQK 226

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801070 557 FSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 609
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) ...
 471-695 4.37e-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: 79.26  E-value: 4.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNLFYLPHGLSIDTDGNYWVTDVA--LHQVFkldphSKEGPLLilgRSMQPGSDQNHFCQPTDVAVepSTGAVFVSD- 547
Cdd:cd14963    50 TGPGEFKYPYGIAVDSDGNIYVADLYngRIQVF-----DPDGKFL---KYFPEKKDRVKLISPAGLAI--DDGKLYVSDv 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 548 GYcnSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKeFVREIKHASFGR 627
Cdd:cd14963   120 KK--HKVIVFDLEGKLLLEFGKPGSE----PGELSYPNGIAVDED-GNIYVADSGNGRIQVFDKNGK-FIKELNGSPDGK 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801070 628 NVFA----ISYIP-GFLFAVN---GKPYFGDQEPVQGFVMNfSSGEIIDVFKpvrkhfdMPHDIVASEDGTVYIGD 695
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; ...
 399-609 8.49e-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: 78.74  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 399 ELDWPgvyllpgqvSGVALDSKNNLVIFHRGDH---VWDGN-SFDSKFVYQQRGLGPI---------EEDTILVIDPNN- 464
Cdd:cd14954    69 QFDRP---------AGVAVNSRGRIIVADKDNHriqVFDLNgRFLLKFGERGTKNGQFnypwgvavdSEGRIYVSDTRNh 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 465 -AEILQSSGKNL------------FYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKegPLLILGrsmQPGSDQNHFCQP 531
Cdd:cd14954   140 rVQVFDSDGQFIrkfgfegagpgqLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQ--FLRFFG---SEGSGNGQFKRP 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801070 532 TDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCF 609
Cdd:cd14954   215 RGVAVDDE-GNIIVADSG-NHRVQVFSPDGEFLCSFGTEGNG----EGQFDRPSGVAVTPD-GRIVVVDRGNHRIQVF 285
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 522-709 1.55e-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: 77.72  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 522 GSDQNHFCQPTDVAVepSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADR 601
Cdd:cd14963     3 GPFGDPLNKPMGVAV--SDGRIYVADTN-NHRVQVFDYEGKFKKSFGGPGTG----PGEFKYPYGIAVDSD-GNIYVADL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 602 ENGRIQCFKTDTKeFVReikhaSFGRNVFAISYI-PGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRK--HFD 678
Cdd:cd14963    75 YNGRIQVFDPDGK-FLK-----YFPEKKDRVKLIsPAGLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEpgELS 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958801070 679 MPHDIVASEDGTVYIGDAHTNTVWKFTLTEK 709
Cdd:cd14963   149 YPNGIAVDEDGNIYVADSGNGRIQVFDKNGK 179
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 470-705 1.76e-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: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 470 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFKldphSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 547
Cdd:cd14957    11 GSGNGQFNTPRGIAVDSAGNIYVADTGNNriQVFT----SSGVYSYSIGSG---GTGSGQFNSPYGIAVD-SNGNIYVAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 548 gYCNSRIVQFSPSGKFVTQWGeeSSGSSprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFkTDTKEFVREIKHASFGR 627
Cdd:cd14957    83 -TDNNRIQVFNSSGVYQYSIG--TGGSG--DGQFNGPYGIAVDSN-GNIYVADTGNHRIQVF-TSSGTFSYSIGSGGTGP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 628 NVFaiSYIPGFLFAVNGKPYFGDQ--EPVQGFVmnfSSGEIIDVF---KPVRKHFDMPHDIVASEDGTVYIGDAHTNTVW 702
Cdd:cd14957   156 GQF--NGPQGIAVDSDGNIYVADTgnHRIQVFT---SSGTFQYTFgssGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQ 230


                  ...
gi 1958801070 703 KFT 705
Cdd:cd14957   231 VFT 233
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 413-609 4.96e-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: 76.54  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 413 SGVALDSKNNLvifhrgdHVWDGNS-----FDSKFVYQQ------RGLGPIEE---------DTILVIDPNNAEI--LQS 470
Cdd:cd14957    68 YGIAVDSNGNI-------YVADTDNnriqvFNSSGVYQYsigtggSGDGQFNGpygiavdsnGNIYVADTGNHRIqvFTS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNL------------FYLPHGLSIDTDGNYWVTDVALH--QVFkldphSKEGPLLilgRSM-QPGSDQNHFCQPTDVA 535
Cdd:cd14957   141 SGTFSysigsggtgpgqFNGPQGIAVDSDGNIYVADTGNHriQVF-----TSSGTFQ---YTFgSSGSGPGQFSDPYGIA 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801070 536 VEpSTGAVFVSDgYCNSRIVQFSPSGKFVTQWGeeSSGSSprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCF 609
Cdd:cd14957   213 VD-SDGNIYVAD-TGNHRIQVFTSSGAYQYSIG--TSGSG--NGQFNYPYGIA-VDNDGKIYVADSNNNRIQVF 279
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
455-705 5.26e-15

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 76.21  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 455 DTILVIDPNNAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNhfcqPTDV 534
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 535 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFVTqwgeessGSSPRPGQFsvPHSLALVPhLDQLCVADRENGRIQCFKTDT 613
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEVTE-------FPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 614 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 693
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246

                         250
                  ....*....|..
gi 1958801070 694 GDAHTNTVWKFT 705
Cdd:COG4257   247 AESGANRIVRFD 258
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 476-707 9.37e-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: 9.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 476 FYLPHGLSIDTDGNYWVTDVALH--QVFKLDPHSKegpllilGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDgYCNSR 553
Cdd:cd14956    12 FKDPRGIAVDADDNVYVADARNGriQVFDKDGTFL-------RRFGTTGDGPGQFGRPRGLAVDK-DGWLYVAD-YWGDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 554 IVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDqLCVADRENGRIQCFKTDTKeFVREIkhasfgrnvfais 633
Cdd:cd14956    83 IQVFTLTGELQTIGGSSGSG----PGQFNAPRGVAVDADGN-LYVADFGNQRIQKFDPDGS-FLRQW------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801070 634 yipgflfavnGKPyfgDQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 707
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 ...
 470-701 7.30e-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: 73.07  E-value: 7.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 470 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkldpHSKEGPLLILGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 547
Cdd:cd14957    58 GTGSGQFNSPYGIAVDSNGNIYVADTDNNriQVF----NSSGVYQYSIGTG---GSGDGQFNGPYGIAVD-SNGNIYVAD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 548 GYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFkTDTKEFVREIKHASFGR 627
Cdd:cd14957   130 TG-NHRIQVFTSSGTFSYSIGSGGTG----PGQFNGPQGIAVDSD-GNIYVADTGNHRIQVF-TSSGTFQYTFGSSGSGP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 628 NVFAISY-IpgflfAV--NGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDA 696
Cdd:cd14957   203 GQFSDPYgI-----AVdsDGNIYVADTgnHRIQvftssgAYQYSIGTSGSGN------GQFNYPYGIAVDNDGKIYVADS 271


                  ....*
gi 1958801070 697 HTNTV 701
Cdd:cd14957   272 NNNRI 276
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 476-701 4.77e-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: 67.57  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 476 FYLPHGLSIDTDGNYWVTDVALH--QVFKLDP--HSKEGpllilgrsmQPGSDQNHFCQPTDVAVEpSTGAVFVSDGYcN 551
Cdd:cd14954    23 LCRPWGVAVDKDGRIIVADRSNNrvQVFDPDGkfLRKFG---------SYGSRDGQFDRPAGVAVN-SRGRIIVADKD-N 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 552 SRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLAlVPHLDQLCVADRENGRIQCFKTDTKeFVREI-------KHAS 624
Cdd:cd14954    92 HRIQVFDLNGRFLLKFGERGTK----NGQFNYPWGVA-VDSEGRIYVSDTRNHRVQVFDSDGQ-FIRKFgfegagpGQLD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 625 FGRNVfAIS-----YIPGF------LFAVNGKP--YFGDQEPVQGFvMNFSSGEIID----------------VFKP--- 672
Cdd:cd14954   166 SPRGV-AVNpdgniVVSDFnnhrlqVFDPDGQFlrFFGSEGSGNGQ-FKRPRGVAVDdegniivadsgnhrvqVFSPdge 243

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958801070 673 -VRK---------HFDMPHDIVASEDGTVYIGDAHTNTV 701
Cdd:cd14954   244 fLCSfgtegngegQFDRPSGVAVTPDGRIVVVDRGNHRI 282
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
401-613 5.42e-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: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 401 DWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGpieeDTILVIDPNNAEILQS--SGKNlfyl 478
Cdd:COG3391    40 ASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGS----GRVSVIDLATGKVVATipVGGG---- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 479 PHGLSIDTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSdqnhfcQPTDVAVEPSTGAVFVSDGYCN--SRIV 555
Cdd:COG3391   112 PRGLAVDPDGGRlYVADSGNGRVSVIDTATGK-----VVATIPVGA------GPHGIAVDPDGKRLYVANSGSNtvSVIV 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801070 556 Q-FSP-SGKFVTQWGEESSgssprpgqfsvPHSLALVPHLDQLCVADRENG-------RIQCFKTDT 613
Cdd:COG3391   181 SvIDTaTGKVVATIPVGGG-----------PVGVAVSPDGRRLYVANRGSNtsnggsnTVSVIDLAT 236
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
479-704 1.92e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 65.43  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 479 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRsmqpgsdqnhFCQPTDVAVEPStGAVFVSDGYcNSRIVQFS 558
Cdd:COG4257    19 PRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGG----------GSGPHGIAVDPD-GNLWFTDNG-NNRIGRID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 559 P-SGKFVTQWGeessgssprPGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKEfVREIKHASFGRNVFAISYIPg 637
Cdd:COG4257    87 PkTGEITTFAL---------PGGGSNPHGIAFDPD-GNLWFTDQGGNRIGRLDPATGE-VTEFPLPTGGAGPYGIAVDP- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801070 638 flfavNGKPYFGDQEPVQGFVMNFSSGEiIDVFKPVRKhFDMPHDIVASEDGTVYIGDAHTNTVWKF 704
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) ...
 472-609 3.04e-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: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 472 GKNLFYLPHGLSIDTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDQNHFCQPTDVAVEPStGAVFVSDGYc 550
Cdd:cd14962    95 AGALFKRPTGIAVDPAGKRlYVVDTLAHKVKVFDLDGRL-----LFDIGKRGSGPGEFNLPTDLAVDRD-GNLYVTDTM- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 551 NSRIVQFSPSGKFVTQWGE-------------------------ESS------------------GSSPRPGQFSVPHSL 587
Cdd:cd14962   168 NFRVQIFDADGKFLRSFGErgdgpgsfarpkgiavdsegniyvvDAAfdnvqifnpegellltvgGPGSGPGEFYLPSGI 247

                         170       180
                  ....*....|....*....|..
gi 1958801070 588 AlVPHLDQLCVADRENGRIQCF 609
Cdd:cd14962   248 A-IDKDDRIYVVDQFNRRIQVF 268
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 476-701 1.23e-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: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 476 FYLPHGLSIDTDGNYWVTDVALHQVFKLDPhskEGPLLILGRSMQPGSDQN------HFCQPTDVAVEPStGAVFVSDGY 549
Cdd:cd14953   131 FNYPTGVAVDAAGNLYVADTGNHRIRKITP---DGVVTTVAGTGGAGYAGDgpataaQFNNPTGVAVDAA-GNLYVADRG 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 550 cNSRIVQFSPSGKFVTQWGEESSGSSPRPG----QFSVPHSLAlVPHLDQLCVADRENGRIqcfktdtkefvREIKHAsf 625
Cdd:cd14953   207 -NHRIRKITPDGVVTTVAGTGTAGFSGDGGataaQLNNPTGVA-VDAAGNLYVADSGNHRI-----------RKITPA-- 271

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801070 626 GRnvfaISYipgflFAVNGKPYFGDQEPVqgfvmnfssgeiidvfKPVRkhFDMPHDIVASEDGTVYIGDAHTNTV 701
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; ...
 457-610 3.33e-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: 61.98  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 457 ILVIDPNN--AEILQSSGKNLFYL-------PHGLSIDTDGNYWVTDVALHQVFKLDPHSKegpllILGRSMQPGSDQNH 527
Cdd:cd14960    77 IIIADYDNkwVSIFSPDGKFKSKIgagklmgPKGVAVDRNGHIIVVDNKACCVFIFQPNGK-----LVTRFGSRGNGDRQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 528 FCQPTDVAVEpSTGAVFVSDgYCNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHlDQLCVADRENGRIQ 607
Cdd:cd14960   152 FAGPHFAAVN-NNNEIIVTD-FHNHSVKVFNAEGEFLFKFGSNGEG----NGQFNAPTGVAVDSN-GNIIVADWGNSRIQ 224


                  ...
gi 1958801070 608 CFK 610
Cdd:cd14960   225 VFD 227
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 457-609 6.05e-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: 60.77  E-value: 6.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 457 ILVIDPNNAEI--LQSSGKNLFYLPH-----------GLSIDtDGNYWVTDVALHQVFKLDPHSKEgpLLILGRsmqPGS 523
Cdd:cd14963    69 IYVADLYNGRIqvFDPDGKFLKYFPEkkdrvklispaGLAID-DGKLYVSDVKKHKVIVFDLEGKL--LLEFGK---PGS 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 524 DQNHFCQPTDVAVEPStGAVFVSD-GycNSRIVQFSPSGKFVTQWGEESSGSS----PR--------------------- 577
Cdd:cd14963   143 EPGELSYPNGIAVDED-GNIYVADsG--NGRIQVFDKNGKFIKELNGSPDGKSgfvnPRgiavdpdgnlyvvdnlshrvy 219

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801070 578 ------------------PGQFSVPHSLALVPHlDQLCVADRENGRIQCF 609
Cdd:cd14963   220 vfdeqgkelftfggrgkdDGQFNLPNGLFIDDD-GRLYVTDRENNRVAVY 268
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 401-613 1.24e-09

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: 59.98  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 401 DWPGVYLLPgqvSGVALDSKNNLVIFHrgdhvwDGNS----FDSKFVYQQRgLGPIEEDT-------------------- 456
Cdd:cd14961     5 GWPGTLNNP---TGVAVTPTGRVVVAD------DGNKriqvFDSDGNCLQQ-FGPKGDAGqdirypldvavtpdghivvt 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 457 ------ILVIDPNnAEILQSSGKNlFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSmqpgsdQNHFCQ 530
Cdd:cd14961    75 dagdrsVKVFSFD-GRLKLFVRKS-FSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLGILKKGQKL------CSQLCR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 531 PTDVAVEPStGAVFVSD-------GYCNSRIVQFSPSGKFVTQWGeeSSGSSPRPGQFSVPHSLAlVPHLDQLCVADREN 603
Cdd:cd14961   147 PRFVAVSRL-GAVAVTEhlfangtRSSSTRVKVFSSGGQLLGQID--SFGLNLVFPSLICASGVA-FDSEGNVIVADTGS 222

                         250
                  ....*....|
gi 1958801070 604 GRIQCFKTDT 613
Cdd:cd14961   223 GAILCLGKPE 232
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
543-701 1.03e-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: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 543 VFVSDGYcNSRIVQFSP-SGKFVTQWgeeSSGSSPrpgqfsvpHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIK 621
Cdd:COG3391    82 LYVANSG-SGRVSVIDLaTGKVVATI---PVGGGP--------RGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 622 hasFGRNVFAISYIP--GFLFAVNgkpyFGDQEpVQGFV--MNFSSGEIIDVFKPvrkhFDMPHDIVASEDG-TVYIGDA 696
Cdd:COG3391   150 ---VGAGPHGIAVDPdgKRLYVAN----SGSNT-VSVIVsvIDTATGKVVATIPV----GGGPVGVAVSPDGrRLYVANR 217


                  ....*
gi 1958801070 697 HTNTV 701
Cdd:COG3391   218 GSNTS 222
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 479-606 2.29e-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: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 479 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLilgrsmqPGSDQNhfcQPTDVAVEpSTGAVFVSDGYcNSRIVQFS 558
Cdd:cd14952    12 PGGVAVDAAGNVYVADSGNNRVLKLAAGSTTQTVL-------PFTGLY---QPQGVAVD-AAGTVYVTDFG-NNRVLKLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801070 559 PsgkfvtqwGEESSGSSPRPGQfSVPHSLAlVPHLDQLCVADRENGRI 606
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 ...
 476-705 4.81e-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: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 476 FYLPHGLSIDTDGNYWVTDVALHQVFKLDPhskEGPLLILGRSMQPGSD-----QNHFCQPTDVAVEPStGAVFVSDGYc 550
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKITP---DGVVTTVAGTGTAGFAdgggaAAQFNTPSGVAVDAA-GNLYVADTG- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 551 NSRIVQFSPSGKFVTQWGEESSGSSPRPG----QFSVPHSLALVPHLDqLCVADRENGRIQcfKTDTKEFVReikhasfg 626
Cdd:cd14953    97 NHRIRKITPDGVVSTLAGTGTAGFSDDGGataaQFNYPTGVAVDAAGN-LYVADTGNHRIR--KITPDGVVT-------- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801070 627 rnVFAISYIPGFLFAVNGkpyfgdqepvqgfvmnfssgeiidvfkpVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFT 705
Cdd:cd14953   166 --TVAGTGGAGYAGDGPA----------------------------TAAQFNNPTGVAVDAAGNLYVADRGNHRIRKIT 214
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
485-644 6.17e-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: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 485 DTDGNY-WVTDVALHQVFKLDPHSKEgplliLGRSMQPGSDqnhfcqPTDVAVEPSTGAVFVSDGYcNSRIVQFSP-SGK 562
Cdd:COG3391    76 GADGRRlYVANSGSGRVSVIDLATGK-----VVATIPVGGG------PRGLAVDPDGGRLYVADSG-NGRVSVIDTaTGK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 563 FVTQWgeeSSGSSprpgqfsvPHSLALVPHLDQLCVADRENGRI----QCFKTDTKEFVREIkhaSFGRNVFAISYIP-- 636
Cdd:COG3391   144 VVATI---PVGAG--------PHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATI---PVGGGPVGVAVSPdg 209


                  ....*...
gi 1958801070 637 GFLFAVNG 644
Cdd:COG3391   210 RRLYVANR 217
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
 522-695 7.80e-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: 51.50  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 522 GSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSgsspRPGQFSVPHSLALVPHLDQLCVADR 601
Cdd:cd14959    15 GSGEGQFNSPSGFCLG-EDEDILVADTN-NHRIQVFDKEGEFKFQFGIPGK----RDGQLWYPNKVAVCRVTGRYVVTDR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 602 ENG--RIQCFkTDTKEFVREikhasfgrnvFAISYI--PGFLfAVNGKPYFGDQEPVQGFVMNFS-SGEIIDVFKpVRKH 676
Cdd:cd14959    89 GNPrhRMQIF-TKRGQFVRK----------FGARYLqhVRGL-TVDAAGHIIVVESKVMRVFIFDeSGNVLKWFD-CSKY 155

                         170
                  ....*....|....*....
gi 1958801070 677 FDMPHDIVASeDGTVYIGD 695
Cdd:cd14959   156 LEEPSDVAVN-DNEIYICD 173
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 479-556 1.30e-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: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801070 479 PHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLilgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQ 556
Cdd:cd14952   180 PSGVAVDTAGNVYVTDHGNNRVLKLAAGSTTPTVL-------PFTGLNG---PLGVAVD-AAGNVYVAD-RGNDRVVK 245
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 409-555 2.36e-06

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: 49.98  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 409 PGQVS---GVALDSKNNLvifhrgdHVWDGNSfdskfvyqQRglgpieedtILVIDPN--NAEILQSS--GKNLFYLPHG 481
Cdd:cd14963   144 PGELSypnGIAVDEDGNI-------YVADSGN--------GR---------IQVFDKNgkFIKELNGSpdGKSGFVNPRG 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801070 482 LSIDTDGNYWVTDVALHQVFKLDPHSKEgpLLILGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDgYCNSRIV 555
Cdd:cd14963   200 IAVDPDGNLYVVDNLSHRVYVFDEQGKE--LFTFG---GRGKDDGQFNLPNGLFIDDD-GRLYVTD-RENNRVA 266
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
594-704 1.32e-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: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 594 DQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVfAISYIPGFLFAVNGKPYFgdqepVQgfVMNFSSGEIIDVFKPv 673
Cdd:COG3391    80 RRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGL-AVDPDGGRLYVADSGNGR-----VS--VIDTATGKVVATIPV- 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958801070 674 rkhFDMPHDIVASEDG-TVYIGDAHTNTVWKF 704
Cdd:COG3391   151 ---GAGPHGIAVDPDGkRLYVANSGSNTVSVI 179
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
 471-564 2.42e-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: 46.88  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkldphSKEGPLLilgrsMQ---PGSDQNHFCQPTDVAVEPSTGAVFV 545
Cdd:cd14959    16 SGEGQFNSPSGFCLGEDEDILVADTNNHriQVF-----DKEGEFK-----FQfgiPGKRDGQLWYPNKVAVCRVTGRYVV 85

                          90       100
                  ....*....|....*....|
gi 1958801070 546 SD-GYCNSRIVQFSPSGKFV 564
Cdd:cd14959    86 TDrGNPRHRMQIFTKRGQFV 105
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 479-606 8.65e-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: 44.89  E-value: 8.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 479 PHGLSIDTDGNYWVTDVALHQVFKLDPhskegpllilGRSMQ---PGSDQNHfcqPTDVAVEPStGAVFVSDGYcNSRIV 555
Cdd:cd14952    96 PTGVAVDAAGNVYVADTGNNRVLKLAA----------GSNTQtvlPFTGLSN---PDGVAVDGA-GNVYVTDTG-NNRVL 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801070 556 QFsPSGkfvtqwgeessGSSPRPGQF---SVPHSLAlVPHLDQLCVADRENGRI 606
Cdd:cd14952   161 KL-AAG-----------STTQTVLPFtglNSPSGVA-VDTAGNVYVTDHGNNRV 201
MALA cd12811
Mala s 1 allergenic protein and similar proteins; This family includes the yeast Malassezia ...
 531-636 9.53e-05

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: 9.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 531 PTDVAVEPStGAVFVSDGYCNSrIVQFSPSGKFVTQWGEESSGSSPRPGqFSvphSLALVPHLDQLCVADRENGRIQCFK 610
Cdd:cd12811   123 FQDSAQDSD-GNSYVVGALPPA-IAKVSPDGKTVTPWFLEAPNGSTRPG-YT---GIAYIPEDNVLLASGGEPGQLTRFD 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958801070 611 TD----TKEFVReIKHASFGRNVFAIsYIP 636
Cdd:cd12811   197 LSsatpTPIPVK-ISGENFGGLDDGE-KLP 224
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 471-615 1.66e-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: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 471 SGKNLFYLPHGLSIDTDGNYWVTD-----ValhQVFKLDphskeGPLLIlGRSMQpGSDQNHFCQPTDVAVEPStGAVFV 545
Cdd:cd14961     5 GWPGTLNNPTGVAVTPTGRVVVADdgnkrI---QVFDSD-----GNCLQ-QFGPK-GDAGQDIRYPLDVAVTPD-GHIVV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801070 546 SDGYCNSRIVqFSPSGK---FVTqwgeessgssprpGQFSVPHSLALVPHlDQLCVADRENGRIQCFKTDTKE 615
Cdd:cd14961    74 TDAGDRSVKV-FSFDGRlklFVR-------------KSFSLPWGVAVNPS-GEILVTDSEAGKLFVLTVDFKL 131
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 409-610 1.67e-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: 44.26  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 409 PGQV---SGVALDSKNNLVIFHRGDHvW------DGnSFDSKFvYQQRGLGPI-----EEDTILVIDpNNA---EILQSS 471
Cdd:cd14960    60 PGQLqrpTGVAVTLNGDIIIADYDNK-WvsifspDG-KFKSKI-GAGKLMGPKgvavdRNGHIIVVD-NKAccvFIFQPN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 472 GK------------NLFYLPHGLSIDTDGNYWVTDVALHQVfKLdpHSKEGPLLILGRSMQPGSDQnhFCQPTDVAVEpS 539
Cdd:cd14960   136 GKlvtrfgsrgngdRQFAGPHFAAVNNNNEIIVTDFHNHSV-KV--FNAEGEFLFKFGSNGEGNGQ--FNAPTGVAVD-S 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801070 540 TGAVFVSDgYCNSRIVQFSPSGKFvtqwgEESSGSSPRPgqFSVPHSLALVPHlDQLCVADRENgriQCFK 610
Cdd:cd14960   210 NGNIIVAD-WGNSRIQVFDSSGSF-----LSYINTSADP--LYGPQGLALTSD-GHVVVADSGN---HCFK 268
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 541-705 7.89e-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: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 541 GAVFVSDGYcNSRIVQFSPSGKFVTQWGEESSGssprPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREI 620
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801070 621 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 697
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205


                  ....*...
gi 1958801070 698 TNTVWKFT 705
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 ...
 581-609 1.17e-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: 1.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958801070 581 FSVPHSLALVPhLDQLCVADRENGRIQCF 609
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 ...
 677-704 3.39e-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: 3.39e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958801070 677 FDMPHDIVASEDGTVYIGDAHTNTVWKF 704
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
452-507 9.89e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 38.85  E-value: 9.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801070 452 IEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHS 507
Cdd:COG4257   206 TGSGRIGRFDPKTGTVTEYPLPGGGARPYGVAVDGDGRVWFAESGANRIVRFDPDT 261
 
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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