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Conserved domains on  [gi|1720354128|ref|XP_030108025|]
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peptidyl-glycine alpha-amidating monooxygenase isoform X1 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
503-810 8.57e-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: 440.55  E-value: 8.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 503 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 583 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 663 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 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 ...
200-346 2.24e-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: 214.04  E-value: 2.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.06e-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: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354128 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
 
Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
503-810 8.57e-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: 440.55  E-value: 8.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 503 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 583 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 663 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 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 ...
200-346 2.24e-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: 214.04  E-value: 2.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.06e-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: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354128 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
560-810 1.61e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 71.97  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 560 DTILVIDPNKAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNhfcqPTDV 639
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 640 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFitqwgeeSSGSSPKPGQFsvPHSLALVPhLNQLCVADRENGRIQCFKTDT 718
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEV-------TEFPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 719 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 798
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246
                         250
                  ....*....|..
gi 1720354128 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 ...
646-855 1.41e-05

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 646 GAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREI 725
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 726 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 802
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354128 803 TNTVWKftLTESRLEVEHrSVKKAGIEVPEIkeaeaVVEPKVKNKPTSSELQK 855
Cdd:pfam17170 206 SPTVYK--IMDGELKPAY-EFDFGGKKNPSI-----DFLKKIETKGNEEFMYD 250
 
Name Accession Description Interval E-value
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
503-810 8.57e-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: 440.55  E-value: 8.57e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 503 EALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSkFVYQQRGlgPIEEDTILVIDPNKaEILQSSGKNLFY 582
Cdd:cd14958     1 MVSSWPSASLKLGQVSGVAVDSLGNGVVFHRGGRVWDANSFDA-NVYVFKG--PIEEDTILVFDPDG-GFLRSWGAGLFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 583 LPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDGYCNSRIVQF 662
Cdd:cd14958    77 MPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEPGSDQTHFCKPTDVAVAP-DGDIFVADGYCNSRIVKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 663 SPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGRnVFAISYIP- 741
Cdd:cd14958   156 SPDGKLLKSWGEPGSG----PGQFNLPHSIALDED-GRVYVADRENGRIQVFDADGK-FLTEWTNPELGR-PYALAIDPd 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 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 ...
200-346 2.24e-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: 214.04  E-value: 2.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 200 IAGMYLMMSV---NTVIPPGEKVVNSDISCHYK--MYPM-----HVFAYRVHTHHLGKVVSGYRVRNGQ-WTLIGRQSPQ 268
Cdd:pfam03712   2 DAGILLLGTVyspKMAIPPGQKVFHLEGYCTIDctDKALpesgiHPFASRLHTHLLGRVVSGYHVRDGQeWPLIGRDNPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 269 LP--QAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYmeakHAVSFMTCTQNVAPDMFRTIP 346
Cdd:pfam03712  82 SPhyQEFYPLEKEVTVLPGDVLAARCTYNTEDRTKVTLGGFTISDEMCNFYIMYY----PRTQLEVCKSSGPPEYLWNYF 157
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
518-809 1.26e-43

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


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 159.41  E-value: 1.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 518 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPNKAEILQ--SSGKNL--FYLPHGLSIDTDG 593
Cdd:cd05819    11 QGIAVDSSGNIYVADTGNN------------------------RIQVFDPDGNFITSfgSFGSGDgqFNEPAGVAVDSDG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 594 NYWVTDVALHQVFKLeprSKEG-PLLVLGRSmqpGSDQNHFCQPTDVAVEPStGAVFVSDgYCNSRIVQFSPSGKFITQW 672
Cdd:cd05819    67 NLYVADTGNHRIQKF---DPDGnFLASFGGS---GDGDGEFNGPRGIAVDSS-GNIYVAD-TGNHRIQKFDPDGEFLTTF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 673 GEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTkEFVREIKHASFGRNVFaiSYIPGFLFAVNGKPY 752
Cdd:cd05819   139 GSGGSG----PGQFNGPTGVAVDSD-GNIYVADTGNHRIQVFDPDG-NFLTTFGSTGTGPGQF--NYPTGIAVDSDGNIY 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354128 753 FGDQEPVQGFVMNFSSGEIID--VFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKF 809
Cdd:cd05819   211 VADSGNNRVQVFDPDGAGFGGngNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
Cu2_monooxygen pfam01082
Copper type II ascorbate-dependent monooxygenase, N-terminal domain; The N and C-terminal ...
63-172 1.06e-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: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128  63 LDIRMPGVT-PKESDTYFCMSMRLP-VDEEAFVIDFKP---RASMDTVHHMLLFGCnmPSSTGSYWFCDEGTCTDKAN-- 135
Cdd:pfam01082   1 FDLLNPNVTvPAKDTTYWCTVFKLPdLTKKHHIIRFEPviqPGNEGLVHHMLLYEC--EGDPNEPSPGYGGDCYSADNmp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720354128 136 --------ILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHY 172
Cdd:pfam01082  79 ddldpcssVIAAWAVGGGGFTYPEEVGLPIGGDGDPRYVMLEVHY 123
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
576-810 1.05e-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: 108.05  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 576 SGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEprSKEGPLLVLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYc 655
Cdd:cd14955   104 SGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFD--SSGTFITKWGSF---GSGDGQFNSPTGIAVD-SAGNVYVADTG- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 656 NSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDTkEFVreikhASFGrnvf 735
Cdd:cd14955   177 NNRIQKFTSTGTFLTKWGSEGSG----DGQFNAPYGIA-VDSAGNVYVADTGNNRIQKFDSSG-TFI-----TKWG---- 241
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354128 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 9.49e-24

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 101.98  E-value: 9.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 560 DTILVIDPNKAEI----LQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKegpllVLGRSMQPGSDQNHFCQ 635
Cdd:cd14956    81 DRIQVFTLTGELQtiggSSGSGPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGS-----FLRQWGGTGIEPGSFNY 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 636 PTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPhLNQLCVADRENGRIQCFK 715
Cdd:cd14956   156 PRGVAVDPD-GTLYVADTY-NDRIQVFDNDGAFLRKWGGRGTG----PGQFNYPYGIAIDP-DGNVFVADFGNNRIQKFT 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 716 TDtkefvreikhasfGRnvfaisyipgFLFAVNGKPyfgdQEPVQgfvmnfssgeiidvfkpvrkhFDMPHDIVASEDGT 795
Cdd:cd14956   229 AD-------------GT----------FLTSWGSPG----TGPGQ---------------------FKNPWGVVVDADGT 260
                         250
                  ....*....|....
gi 1720354128 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 ...
518-714 1.16e-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: 96.11  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 518 SGVALDSKNNLvifhrgdHVWDGNS-----FDS--KFVYQQRGLGpieedtilvidpnkaeilqsSGKNLFYLPHGLSID 590
Cdd:cd14955   113 SGIAVDSAGNV-------YVTDSGNnriqkFDSsgTFITKWGSFG--------------------SGDGQFNSPTGIAVD 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 591 TDGNYWVTDVALHQVFKLEPRSkeGPLLVLGRsmqPGSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFIT 670
Cdd:cd14955   166 SAGNVYVADTGNNRIQKFTSTG--TFLTKWGS---EGSGDGQFNAPYGIAVD-SAGNVYVADTG-NNRIQKFDSSGTFIT 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720354128 671 QWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 714
Cdd:cd14955   239 KWGSEGSG----DGQFNSPSGIA-VDSAGNVYVADSGNNRIQKF 277
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
627-812 3.70e-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: 94.57  E-value: 3.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 627 GSDQNHFCQPTDVAVEpSTGAVFVSDgYCNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADR 706
Cdd:cd14955     9 GSGDGQFNSPSGIAVD-SAGNVYVAD-TGNNRIQKFDSTGTFLTKWGSSGSG----DGQFYSPTGIAVDSDGN-VYVADT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 707 ENGRIQCFkTDTKEFVReiKHASFGRNVFAISYIPGFLFAVNGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpv 778
Cdd:cd14955    82 GNHRIQKF-DSTGTFLT--KWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSgnNRIQkfdssgTFITKWGSFGSGD----- 153
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720354128 779 rKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT 812
Cdd:cd14955   154 -GQFNSPTGIAVDSAGNVYVADTGNNRIQKFTST 186
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
514-714 2.17e-18

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 86.18  E-value: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 514 PGQ---VSGVALDSKNNLVI----FHRGDHVwdgnSFDSKFVYQ--QRGLGPIEedtilvidpnkaeilqssgknlFYLP 584
Cdd:cd14956   103 PGQfnaPRGVAVDADGNLYVadfgNQRIQKF----DPDGSFLRQwgGTGIEPGS----------------------FNYP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 585 HGLSIDTDGNYWVTDVALH--QVFKLEPRskegPLLVLGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQF 662
Cdd:cd14956   157 RGVAVDPDGTLYVADTYNDriQVFDNDGA----FLRKWG---GRGTGPGQFNYPYGIAIDPD-GNVFVADFG-NNRIQKF 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 663 SPSGKFITQWGEESSGsspkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 714
Cdd:cd14956   228 TADGTFLTSWGSPGTG----PGQFKNPWGVV-VDADGTVYVADSNNNRVQRF 274
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
576-800 4.24e-17

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


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 82.34  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 576 SGKNLFYLPHGLSIDTDGNYWVTDVA--LHQVFkleprSKEGPLLvlgRSMQPGSDQNHFCQPTDVAVepSTGAVFVSD- 652
Cdd:cd14963    50 TGPGEFKYPYGIAVDSDGNIYVADLYngRIQVF-----DPDGKFL---KYFPEKKDRVKLISPAGLAI--DDGKLYVSDv 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 653 GYcnSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKeFVREIKHASFGR 732
Cdd:cd14963   120 KK--HKVIVFDLEGKLLLEFGKPGSE----PGELSYPNGIAVDED-GNIYVADSGNGRIQVFDKNGK-FIKELNGSPDGK 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354128 733 NVFA----ISYIP-GFLFAVN---GKPYFGDQEPVQGFVMNfSSGEIIDVFKpvrkhfdMPHDIVASEDGTVYIGD 800
Cdd:cd14963   192 SGFVnprgIAVDPdGNLYVVDnlsHRVYVFDEQGKELFTFG-GRGKDDGQFN-------LPNGLFIDDDGRLYVTD 259
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
577-732 7.89e-17

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


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 81.86  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 577 GKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPrsKEGPLLVLGRSMQpgsdqnhFCQPTDVAVEPSTGAVFVSDGYcN 656
Cdd:cd14962    52 GPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDR--DGKFLRAIGAGAL-------FKRPTGIAVDPAGKRLYVVDTL-A 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354128 657 SRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFKTDTKeFVReikhaSFGR 732
Cdd:cd14962   122 HKVKVFDLDGRLLFDIGKRGSG----PGEFNLPTDLAVDRDGN-LYVTDTMNFRVQIFDADGK-FLR-----SFGE 186
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
575-810 1.44e-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: 81.16  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 575 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLVLGRSmqPGSDQNHFCQPTDVAVEpSTGAVFVSD 652
Cdd:cd14957    11 GSGNGQFNTPRGIAVDSAGNIYVADTGNNriQVF-----TSSGVYSYSIGS--GGTGSGQFNSPYGIAVD-SNGNIYVAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 653 gYCNSRIVQFSPSGKFITQWGeeSSGSSpkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFkTDTKEFVREIKHASFGR 732
Cdd:cd14957    83 -TDNNRIQVFNSSGVYQYSIG--TGGSG--DGQFNGPYGIAVDSNGN-IYVADTGNHRIQVF-TSSGTFSYSIGSGGTGP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 733 NVFaiSYIPGFLFAVNGKPYFGDQ--EPVQGFVmnfSSGEIIDVF---KPVRKHFDMPHDIVASEDGTVYIGDAHTNTVW 807
Cdd:cd14957   156 GQF--NGPQGIAVDSDGNIYVADTgnHRIQVFT---SSGTFQYTFgssGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQ 230

                  ...
gi 1720354128 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) ...
627-831 2.48e-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: 80.03  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 627 GSDQNHFCQPTDVAVepSTGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHlNQLCVADR 706
Cdd:cd14963     3 GPFGDPLNKPMGVAV--SDGRIYVADTN-NHRVQVFDYEGKFKKSFGGPGTG----PGEFKYPYGIAVDSD-GNIYVADL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 707 ENGRIQCFKTDTKeFVReikhaSFGRNVFAISYI-PGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRK--HFD 783
Cdd:cd14963    75 YNGRIQVFDPDGK-FLK-----YFPEKKDRVKLIsPAGLAIDDGKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEpgELS 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720354128 784 MPHDIVASEDGTVYIGDAHTNTVWKFTLTESRL-EVEHRSVKKAGIEVP 831
Cdd:cd14963   149 YPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIkELNGSPDGKSGFVNP 197
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
519-714 1.08e-15

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


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 78.74  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 519 GVALDSKNNLVIFHRGDH---VWDGN-SFDSKFVYQQRGLGPIEEdtilvidpnkaeilqssgknlfylPHGLSIDTDGN 594
Cdd:cd14954   122 GVAVDSEGRIYVSDTRNHrvqVFDSDgQFIRKFGFEGAGPGQLDS------------------------PRGVAVNPDGN 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 595 YWVTDVALHQVFKLEPRSKegPLLVLGrsmQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGE 674
Cdd:cd14954   178 IVVSDFNNHRLQVFDPDGQ--FLRFFG---SEGSGNGQFKRPRGVAVDDE-GNIIVADSG-NHRVQVFSPDGEFLCSFGT 250
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720354128 675 ESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCF 714
Cdd:cd14954   251 EGNG----EGQFDRPSGVAVTPDGR-IVVVDRGNHRIQVF 285
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
575-714 1.88e-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: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 575 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGpllVLGRSM-QPGSDQNHFCQPTDVAVEpSTGAVFVS 651
Cdd:cd14957   152 GTGPGQFNGPQGIAVDSDGNIYVADTGNHriQVF-----TSSG---TFQYTFgSSGSGPGQFSDPYGIAVD-SDGNIYVA 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354128 652 DgYCNSRIVQFSPSGKFITQWGeeSSGSSpkPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 714
Cdd:cd14957   223 D-TGNHRIQVFTSSGAYQYSIG--TSGSG--NGQFNYPYGIA-VDNDGKIYVADSNNNRIQVF 279
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
581-812 2.10e-15

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 77.71  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 581 FYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlGRSMQPGSDQNHFCQPTDVAVEPsTGAVFVSDgYCNSR 658
Cdd:cd14956    12 FKDPRGIAVDADDNVYVADARNGriQVF-----DKDGTFL--RRFGTTGDGPGQFGRPRGLAVDK-DGWLYVAD-YWGDR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 659 IVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFKTDTKeFVREIkhasfgrnvfais 738
Cdd:cd14956    83 IQVFTLTGELQTIGGSSGSG----PGQFNAPRGVAVDADGN-LYVADFGNQRIQKFDPDGS-FLRQW------------- 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354128 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 4.50e-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: 4.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 575 SSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFKleprSKEGPLLVLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSD 652
Cdd:cd14957    58 GTGSGQFNSPYGIAVDSNGNIYVADTDNNriQVFN----SSGVYQYSIGTG---GSGDGQFNGPYGIAVD-SNGNIYVAD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 653 GYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFKTDTkEFVREIKHASFGR 732
Cdd:cd14957   130 TG-NHRIQVFTSSGTFSYSIGSGGTG----PGQFNGPQGIAVDSDGN-IYVADTGNHRIQVFTSSG-TFQYTFGSSGSGP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 733 NVFAISY-IpgflfAV--NGKPYFGDQ--EPVQ------GFVMNFSSGEIIDvfkpvrKHFDMPHDIVASEDGTVYIGDA 801
Cdd:cd14957   203 GQFSDPYgI-----AVdsDGNIYVADTgnHRIQvftssgAYQYSIGTSGSGN------GQFNYPYGIAVDNDGKIYVADS 271

                  ....*
gi 1720354128 802 HTNTV 806
Cdd:cd14957   272 NNNRI 276
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
560-810 1.61e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 71.97  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 560 DTILVIDPNKAEILQSSgKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNhfcqPTDV 639
Cdd:COG4257    38 GRIGRLDPATGEFTEYP-LGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE-----ITTFALPGGGSN----PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 640 AVEPStGAVFVSDGYcNSRIVQFSP-SGKFitqwgeeSSGSSPKPGQFsvPHSLALVPhLNQLCVADRENGRIQCFKTDT 718
Cdd:COG4257   108 AFDPD-GNLWFTDQG-GNRIGRLDPaTGEV-------TEFPLPTGGAG--PYGIAVDP-DGNLWVTDFGANAIGRIDPDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 719 KEFVREIKHASFGRNVfaisyipGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFdmPHDIVASEDGTVYI 798
Cdd:COG4257   176 GTLTEYALPTPGAGPR-------GLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGAR--PYGVAVDGDGRVWF 246
                         250
                  ....*....|..
gi 1720354128 799 GDAHTNTVWKFT 810
Cdd:COG4257   247 AESGANRIVRFD 258
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
581-806 6.93e-13

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


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 70.27  E-value: 6.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 581 FYLPHGLSIDTDGNYWVTDVALH--QVFKleprsKEGPLL-VLGRSmqpGSDQNHFCQPTDVAVEpSTGAVFVSDGYcNS 657
Cdd:cd14954    23 LCRPWGVAVDKDGRIIVADRSNNrvQVFD-----PDGKFLrKFGSY---GSRDGQFDRPAGVAVN-SRGRIIVADKD-NH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 658 RIVQFSPSGKFITQWGEESSgsspKPGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDTKeFVREI-------KHASF 730
Cdd:cd14954    93 RIQVFDLNGRFLLKFGERGT----KNGQFNYPWGVA-VDSEGRIYVSDTRNHRVQVFDSDGQ-FIRKFgfegagpGQLDS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 731 GRNVfAIS-----YIPGF------LFAVNGKP--YFGDQEPVQGFvMNFSSGEIID----------------VFKP---- 777
Cdd:cd14954   167 PRGV-AVNpdgniVVSDFnnhrlqVFDPDGQFlrFFGSEGSGNGQ-FKRPRGVAVDdegniivadsgnhrvqVFSPdgef 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720354128 778 VRK---------HFDMPHDIVASEDGTVYIGDAHTNTV 806
Cdd:cd14954   245 LCSfgtegngegQFDRPSGVAVTPDGRIVVVDRGNHRI 282
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
514-714 5.13e-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: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 514 PGQV---SGVALDSKNNLVIFHRGDH---VWDGN-SFDSKFvyQQRGlgpieedtilvidpnkaeilQSSGKnlFYLPHG 586
Cdd:cd14954    67 DGQFdrpAGVAVNSRGRIIVADKDNHriqVFDLNgRFLLKF--GERG--------------------TKNGQ--FNYPWG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 587 LSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlgrsMQPGSDQN---HFCQPTDVAVEPsTGAVFVSDgYCNSRIVQ 661
Cdd:cd14954   123 VAVDSEGRIYVSDTRNHrvQVF-----DSDGQFI-----RKFGFEGAgpgQLDSPRGVAVNP-DGNIVVSD-FNNHRLQV 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354128 662 FSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLcVADRENGRIQCF 714
Cdd:cd14954   191 FDPDGQFLRFFGSEGSG----NGQFKRPRGVAVDDEGNII-VADSGNHRVQVF 238
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
584-809 1.45e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 66.20  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRsmqpgsdqnhFCQPTDVAVEPStGAVFVSDGYcNSRIVQFS 663
Cdd:COG4257    19 PRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGG----------GSGPHGIAVDPD-GNLWFTDNG-NNRIGRID 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 664 PSGKFITQWgeessgssPKPGQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKEfVREIKHASFGRNVFAISYIPgf 743
Cdd:COG4257    87 PKTGEITTF--------ALPGGGSNPHGIAFDPD-GNLWFTDQGGNRIGRLDPATGE-VTEFPLPTGGAGPYGIAVDP-- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354128 744 lfavNGKPYFGDQEPVQGFVMNFSSGEiIDVFKPVRKhFDMPHDIVASEDGTVYIGDAHTNTVWKF 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) ...
562-714 4.94e-11

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


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 64.53  E-value: 4.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 562 ILVIDPNKAEILQSSGKNLFYLPHGLSIDTDGNY-WVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDQNHFCQPTDVA 640
Cdd:cd14962    80 VFVFDRDGKFLRAIGAGALFKRPTGIAVDPAGKRlYVVDTLAHKVKVFDLDGRL-----LFDIGKRGSGPGEFNLPTDLA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 641 VEPStGAVFVSDGYcNSRIVQFSPSGKFITQWGE-------------------------ESS------------------ 677
Cdd:cd14962   155 VDRD-GNLYVTDTM-NFRVQIFDADGKFLRSFGErgdgpgsfarpkgiavdsegniyvvDAAfdnvqifnpegellltvg 232
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720354128 678 GSSPKPGQFSVPHSLAlVPHLNQLCVADRENGRIQCF 714
Cdd:cd14962   233 GPGSGPGEFYLPSGIA-IDKDDRIYVVDQFNRRIQVF 268
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
507-718 2.02e-10

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


Pssm-ID: 271331 [Multi-domain]  Cd Length: 273  Bit Score: 62.68  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 507 WPGVYLLPgqvSGVALDSKNNLVIFHrgdhvwDGNS----FDSKFVYQQRgLGPIEEDT--------------------- 561
Cdd:cd14961     6 WPGTLNNP---TGVAVTPTGRVVVAD------DGNKriqvFDSDGNCLQQ-FGPKGDAGqdirypldvavtpdghivvtd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 562 -----ILVIDPNKaEILQSSGKNlFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSmqpgsdQNHFCQP 636
Cdd:cd14961    76 agdrsVKVFSFDG-RLKLFVRKS-FSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLGILKKGQKL------CSQLCRP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 637 TDVAVEPStGAVFVSD-------GYCNSRIVQFSPSGKFITQWGeeSSGSSPKPGQFSVPHSLAlVPHLNQLCVADRENG 709
Cdd:cd14961   148 RFVAVSRL-GAVAVTEhlfangtRSSSTRVKVFSSGGQLLGQID--SFGLNLVFPSLICASGVA-FDSEGNVIVADTGSG 223

                  ....*....
gi 1720354128 710 RIQCFKTDT 718
Cdd:cd14961   224 AILCLGKPE 232
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
518-711 3.33e-10

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


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 62.55  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 518 SGVALDSKNNLVIFHRGDHvwdgnsfdskfvyqqrglgpieedTILVIDPN-KAEILQSSGK----------NLFYLPHG 586
Cdd:cd14953    26 SGVAVDAAGNLYVADRGNH------------------------RIRKITPDgVVTTVAGTGTagfadgggaaAQFNTPSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 587 LSIDTDGNYWVTDVALHQVFKLEPrskEGPLLVL------GRSMQPGSDQNHFCQPTDVAVEPStGAVFVSDGYcNSRIV 660
Cdd:cd14953    82 VAVDAAGNLYVADTGNHRIRKITP---DGVVSTLagtgtaGFSDDGGATAAQFNYPTGVAVDAA-GNLYVADTG-NHRIR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720354128 661 QFSPSGKFITQWGEESSGSSP-KPG---QFSVPHSLALVPHLNqLCVADRENGRI 711
Cdd:cd14953   157 KITPDGVVTTVAGTGGAGYAGdGPAtaaQFNNPTGVAVDAAGN-LYVADRGNHRI 210
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
584-715 1.99e-09

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


Pssm-ID: 271330 [Multi-domain]  Cd Length: 274  Bit Score: 59.67  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKegpllVLGRSMQPGSDQNHFCQPTDVAVEpSTGAVFVSDgYCNSRIVQFS 663
Cdd:cd14960   108 PKGVAVDRNGHIIVVDNKACCVFIFQPNGK-----LVTRFGSRGNGDRQFAGPHFAAVN-NNNEIIVTD-FHNHSVKVFN 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 664 PSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNqLCVADRENGRIQCFK 715
Cdd:cd14960   181 AEGEFLFKFGSNGEG----NGQFNAPTGVAVDSNGN-IIVADWGNSRIQVFD 227
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
508-714 2.82e-09

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


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 59.23  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 508 PGVYLLPgqvSGVALDSKNNLVI---FHRGDHVWD--GNsFDSKFVYQQRGLGP-------IEEDTILVID--PNKAEIL 573
Cdd:cd14963    52 PGEFKYP---YGIAVDSDGNIYVadlYNGRIQVFDpdGK-FLKYFPEKKDRVKLispaglaIDDGKLYVSDvkKHKVIVF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 574 QSSGKNLFYL------------PHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLL--VLGRSMQPGSdqnhFCQPT 637
Cdd:cd14963   128 DLEGKLLLEFgkpgsepgelsyPNGIAVDEDGNIYVADSGNGriQVF-----DKNGKFIkeLNGSPDGKSG----FVNPR 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354128 638 DVAVEPsTGAVFVSDGYCNsRIVQFSPSGKFITQWGeeSSGSSPkpGQFSVPHSLALVPHlNQLCVADRENGRIQCF 714
Cdd:cd14963   199 GIAVDP-DGNLYVVDNLSH-RVYVFDEQGKELFTFG--GRGKDD--GQFNLPNGLFIDDD-GRLYVTDRENNRVAVY 268
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
648-806 1.04e-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: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 648 VFVSDGYcNSRIVQFSP-SGKFITQWgeeSSGSSPkpgqfsvpHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREIK 726
Cdd:COG3391    82 LYVANSG-SGRVSVIDLaTGKVVATI---PVGGGP--------RGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 727 hasFGRNVFAISYIP--GFLFAVNgkpyFGDQEpVQGFV--MNFSSGEIIDVFKPvrkhFDMPHDIVASEDG-TVYIGDA 801
Cdd:COG3391   150 ---VGAGPHGIAVDPdgKRLYVAN----SGSNT-VSVIVsvIDTATGKVVATIPV----GGGPVGVAVSPDGrRLYVANR 217

                  ....*
gi 1720354128 802 HTNTV 806
Cdd:COG3391   218 GSNTS 222
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
580-711 2.09e-07

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


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 54.07  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 580 LFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPllVLGRSMQPGSDQNH-----FCQPTDVAVEpSTGAVFVSDgY 654
Cdd:cd14953   185 QFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVTT--VAGTGTAGFSGDGGataaqLNNPTGVAVD-AAGNLYVAD-S 260
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354128 655 CNSRIVQFSPSGKFIT----QWGEESSGSSPKPGQFSVPHSLALVPHLNqLCVADRENGRI 711
Cdd:cd14953   261 GNHRIRKITPAGVVTTvaggGAGFSGDGGPATSAQFNNPTGVAVDAAGN-LYVADTGNNRI 320
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
581-810 2.25e-07

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


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 53.69  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 581 FYLPHGLSIDTDGNYWVTDVALHQVFKLeprSKEGPLLVLGRSMQPGSD-----QNHFCQPTDVAVEPStGAVFVSDGYc 655
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKI---TPDGVVTTVAGTGTAGFAdgggaAAQFNTPSGVAVDAA-GNLYVADTG- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 656 NSRIVQFSPSGKFITQWGEESSGSSPKPG----QFSVPHSLALVPHLNqLCVADRENGRIQcfKTDTKEFVReikhasfg 731
Cdd:cd14953    97 NHRIRKITPDGVVSTLAGTGTAGFSDDGGataaQFNYPTGVAVDAAGN-LYVADTGNHRIR--KITPDGVVT-------- 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354128 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 2.90e-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: 53.04  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 627 GSDQNHFCQPTDVAVEpSTGAVFVSDGYcNSRIVQFSPSGKFITQWGEESSgsspKPGQFSVPHSLALVPHLNQLCVADR 706
Cdd:cd14959    15 GSGEGQFNSPSGFCLG-EDEDILVADTN-NHRIQVFDKEGEFKFQFGIPGK----RDGQLWYPNKVAVCRVTGRYVVTDR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 707 ENG--RIQCFkTDTKEFVREikhasfgrnvFAISYI--PGFLfAVNGKPYFGDQEPVQGFVMNFS-SGEIIDVFKpVRKH 781
Cdd:cd14959    89 GNPrhRMQIF-TKRGQFVRK----------FGARYLqhVRGL-TVDAAGHIIVVESKVMRVFIFDeSGNVLKWFD-CSKY 155
                         170
                  ....*....|....*....
gi 1720354128 782 FDMPHDIVASeDGTVYIGD 800
Cdd:cd14959   156 LEEPSDVAVN-DNEIYICD 173
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
584-711 3.46e-07

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


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 52.60  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLvlgrsmqPGSDQNhfcQPTDVAVEpSTGAVFVSDGYcNSRIVQFS 663
Cdd:cd14952    12 PGGVAVDAAGNVYVADSGNNRVLKLAAGSTTQTVL-------PFTGLY---QPQGVAVD-AAGTVYVTDFG-NNRVLKLA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 664 PsgkfitqwgeessGSS-PKPGQF---SVPHSLALVPHLNqLCVADRENGRI 711
Cdd:cd14952    80 A-------------GSTtQTVLPFtglNDPTGVAVDAAGN-VYVADTGNNRV 117
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
584-661 2.06e-06

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


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 50.28  E-value: 2.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEgpLLVLgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQ 661
Cdd:cd14952   180 PSGVAVDTAGNVYVTDHGNNRVLKLAAGSTT--PTVL-----PFTGLNG---PLGVAVD-AAGNVYVAD-RGNDRVVK 245
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
590-749 2.61e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 49.69  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 590 DTDGNY-WVTDVALHQVFKLEPRSKEgpllvLGRSMQPGSDqnhfcqPTDVAVEPSTGAVFVSDGYcNSRIVQFSP-SGK 667
Cdd:COG3391    76 GADGRRlYVANSGSGRVSVIDLATGK-----VVATIPVGGG------PRGLAVDPDGGRLYVADSG-NGRVSVIDTaTGK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 668 FITQWgeeSSGSSpkpgqfsvPHSLALVPHLNQLCVADRENGRI----QCFKTDTKEFVREIkhaSFGRNVFAISYIP-- 741
Cdd:COG3391   144 VVATI---PVGAG--------PHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKVVATI---PVGGGPVGVAVSPdg 209

                  ....*...
gi 1720354128 742 GFLFAVNG 749
Cdd:COG3391   210 RRLYVANR 217
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
699-809 8.99e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.15  E-value: 8.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 699 NQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVfAISYIPGFLFAVNGKPYFgdqepVQgfVMNFSSGEIIDVFKPv 778
Cdd:COG3391    80 RRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGL-AVDPDGGRLYVADSGNGR-----VS--VIDTATGKVVATIPV- 150
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720354128 779 rkhFDMPHDIVASEDG-TVYIGDAHTNTVWKF 809
Cdd:COG3391   151 ---GAGPHGIAVDPDGkRLYVANSGSNTVSVI 179
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
646-855 1.41e-05

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 646 GAVFVSDGYcNSRIVQFSPSGKFITQWGEESSGsspkPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREI 725
Cdd:pfam17170  54 DRIFVFDSN-TNNLFVFDKKGKFVRQIGAQGNG----PGEYLQINDFIIDKSNNSIYILDFMQNKILTYDLDGYSFIGEI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 726 KHASFgrNVFAISYIPGFLFAVNGKPYFGDQEPVQgFVMNFSSGEIIDVFKPVRKHFDM---PHDIVASEDGTVYIGDAH 802
Cdd:pfam17170 129 NLDLL--PSDCCQLDKGKLAFDSSGFDDGKRSGFY-LVITDELGNIISGFFPAEFTLGIlfnSSVPFYEYGDNIYFYPYY 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720354128 803 TNTVWKftLTESRLEVEHrSVKKAGIEVPEIkeaeaVVEPKVKNKPTSSELQK 855
Cdd:pfam17170 206 SPTVYK--IMDGELKPAY-EFDFGGKKNPSI-----DFLKKIETKGNEEFMYD 250
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
668-810 1.53e-05

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


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 47.96  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 668 FITQWGEESSGSspkpGQFSVPHSLAlVPHLNQLCVADRENGRIQCFKTDtkefvreikhasfgrnvfaisyipGFLFAV 747
Cdd:cd14955     1 FVTQWGSYGSGD----GQFNSPSGIA-VDSAGNVYVADTGNNRIQKFDST------------------------GTFLTK 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354128 748 NGKPYFGDqepvqgfvmnfssGEiidvfkpvrkhFDMPHDIVASEDGTVYIGDAHTNTVWKFT 810
Cdd:cd14955    52 WGSSGSGD-------------GQ-----------FYSPTGIAVDSDGNVYVADTGNHRIQKFD 90
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
576-669 3.27e-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: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 576 SGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGPLLvlgrsMQ---PGSDQNHFCQPTDVAVEPSTGAVFV 650
Cdd:cd14959    16 SGEGQFNSPSGFCLGEDEDILVADTNNHriQVF-----DKEGEFK-----FQfgiPGKRDGQLWYPNKVAVCRVTGRYVV 85
                          90       100
                  ....*....|....*....|
gi 1720354128 651 SD-GYCNSRIVQFSPSGKFI 669
Cdd:cd14959    86 TDrGNPRHRMQIFTKRGQFV 105
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
514-715 3.33e-05

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


Pssm-ID: 271330 [Multi-domain]  Cd Length: 274  Bit Score: 46.57  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 514 PGQV---SGVALDSKNNLVIFHRGDHvW------DGnSFDSKFvYQQRGLGPI-----EEDTILVIDpNKA---EILQSS 576
Cdd:cd14960    60 PGQLqrpTGVAVTLNGDIIIADYDNK-WvsifspDG-KFKSKI-GAGKLMGPKgvavdRNGHIIVVD-NKAccvFIFQPN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 577 GK------------NLFYLPHGLSIDTDGNYWVTDVALHQVfKLepRSKEGPLLVLGRSMQPGSDQnhFCQPTDVAVEpS 644
Cdd:cd14960   136 GKlvtrfgsrgngdRQFAGPHFAAVNNNNEIIVTDFHNHSV-KV--FNAEGEFLFKFGSNGEGNGQ--FNAPTGVAVD-S 209
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354128 645 TGAVFVSDgYCNSRIVQFSPSGKFitqwgEESSGSSPKPgqFSVPHSLALVPHlNQLCVADRENgriQCFK 715
Cdd:cd14960   210 NGNIIVAD-WGNSRIQVFDSSGSF-----LSYINTSADP--LYGPQGLALTSD-GHVVVADSGN---HCFK 268
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
584-661 7.85e-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: 7.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSkeGPLLVLgrsmqPGSDQNHfcqPTDVAVEPStGAVFVSDGYcNSRIVQ 661
Cdd:cd14952    96 PTGVAVDAAGNVYVADTGNNRVLKLAAGS--NTQTVL-----PFTGLSN---PDGVAVDGA-GNVYVTDTG-NNRVLK 161
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
627-720 7.92e-05

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


Pssm-ID: 271331 [Multi-domain]  Cd Length: 273  Bit Score: 45.73  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 627 GSDQNHFCQPTDVAVEPsTGAVFVSD-GycNSRIVQFSPSGKFITQWGEESSGSSPKP---------------------- 683
Cdd:cd14961     4 GGWPGTLNNPTGVAVTP-TGRVVVADdG--NKRIQVFDSDGNCLQQFGPKGDAGQDIRypldvavtpdghivvtdagdrs 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720354128 684 ---------------GQFSVPHSLALVPHlNQLCVADRENGRIQCFKTDTKE 720
Cdd:cd14961    81 vkvfsfdgrlklfvrKSFSLPWGVAVNPS-GEILVTDSEAGKLFVLTVDFKL 131
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
574-663 1.87e-04

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


Pssm-ID: 271327 [Multi-domain]  Cd Length: 280  Bit Score: 44.56  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 574 QSSGKNLFYLPHGLSIDTDGNYWVTDVALH--QVFkleprSKEGpllVLGRSM-QPGSDQNHFCQPTDVAVEpSTGAVFV 650
Cdd:cd14957   198 SGSGPGQFSDPYGIAVDSDGNIYVADTGNHriQVF-----TSSG---AYQYSIgTSGSGNGQFNYPYGIAVD-NDGKIYV 268
                          90
                  ....*....|...
gi 1720354128 651 SDGYcNSRIVQFS 663
Cdd:cd14957   269 ADSN-NNRIQVFN 280
MALA cd12811
Mala s 1 allergenic protein and similar proteins; This family includes the yeast Malassezia ...
636-741 5.24e-04

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


Pssm-ID: 411995 [Multi-domain]  Cd Length: 304  Bit Score: 43.39  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 636 PTDVAVEPStGAVFVSDGYCNSrIVQFSPSGKFITQWGEESSGSSPKPGqFSvphSLALVPHLNQLCVADRENGRIQCFK 715
Cdd:cd12811   123 FQDSAQDSD-GNSYVVGALPPA-IAKVSPDGKTVTPWFLEAPNGSTRPG-YT---GIAYIPEDNVLLASGGEPGQLTRFD 196
                          90       100       110
                  ....*....|....*....|....*....|
gi 1720354128 716 TD----TKEFVReIKHASFGRNVFAIsYIP 741
Cdd:cd12811   197 LSsatpTPIPVK-ISGENFGGLDDGE-KLP 224
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
686-714 7.52e-04

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 7.52e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720354128 686 FSVPHSLALVPhLNQLCVADRENGRIQCF 714
Cdd:pfam01436   1 FNRPHGVAVDS-NGDIYVADSENHRVQVF 28
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
584-664 1.88e-03

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


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 41.04  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 584 PHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLvlgrsmqPGSDQNHfcqPTDVAVEpSTGAVFVSDgYCNSRIVQFS 663
Cdd:cd14952   138 PDGVAVDGAGNVYVTDTGNNRVLKLAAGSTTQTVL-------PFTGLNS---PSGVAVD-TAGNVYVTD-HGNNRVLKLA 205

                  .
gi 1720354128 664 P 664
Cdd:cd14952   206 A 206
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
782-809 3.52e-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: 3.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1720354128 782 FDMPHDIVASEDGTVYIGDAHTNTVWKF 809
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
558-657 4.24e-03

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.06  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354128 558 EEDTILVIDPNKAEILQS--SGKNlfylPHGLSIDTDGNY-WVTDVALHQ----VFKLEPRSKEgpllVLGRsMQPGSdq 630
Cdd:COG3391   130 GNGRVSVIDTATGKVVATipVGAG----PHGIAVDPDGKRlYVANSGSNTvsviVSVIDTATGK----VVAT-IPVGG-- 198
                          90       100
                  ....*....|....*....|....*..
gi 1720354128 631 nhfcQPTDVAVEPSTGAVFVSDGYCNS 657
Cdd:COG3391   199 ----GPVGVAVSPDGRRLYVANRGSNT 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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