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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTK 539
Cdd:cd05819   115 IYVADTGNHRIQKFDPDGEFLTTFGS---GGSGPGQFNGPTGVAVDSDGNIYVADTGNHRIQVFDPDGNFLttfGSTGTG 191

                          90
                  ....*....|....*
gi 1351339760 540 SDNIELPISVAVNSN 554
Cdd:cd05819   192 PGQFNYPTGIAVDSD 206

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760  69 EQLRHILDKAQCCD---KHDSELLTFYCEE-------DDTVACRDCILETHSKHDfKKIGDVVKVQREL--IQAKFKCLT 136
Cdd:pfam05701  80 EELKLNLERAQTEEaqaKQDSELAKLRVEEmeqgiadEASVAAKAQLEVAKARHA-AAVAELKSVKEELesLRKEYASLV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 137 TEKLTRFEKAEKVIM---ETEDEVTE-----NQTK-VLRL-------VDSQKL--AMTKEINKNskTFKREIKdyyqQVE 198
Cdd:pfam05701 159 SERDIAIKRAEEAVSaskEIEKTVEEltielIATKeSLESahaahleAEEHRIgaALAREQDKL--NWEKELK----QAE 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 199 KDVRQQTDAYL--TSVKQHLETYETKIQS------DYTEMKrfINDKSREITTEVKALTSTQMKTLEAKKDKQEMnKISI 270
Cdd:pfam05701 233 EELQRLNQQLLsaKDLKSKLETASALLLDlkaelaAYMESK--LKEEADGEGNEKKTSTSIQAALASAKKELEEV-KANI 309

                         250
                  ....*....|.
gi 1351339760 271 QSIRDFAQQLT 281
Cdd:pfam05701 310 EKAKDEVNCLR 320

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTK 539
Cdd:cd05819   115 IYVADTGNHRIQKFDPDGEFLTTFGS---GGSGPGQFNGPTGVAVDSDGNIYVADTGNHRIQVFDPDGNFLttfGSTGTG 191

                          90
                  ....*....|....*
gi 1351339760 540 SDNIELPISVAVNSN 554
Cdd:cd05819   192 PGQFNYPTGIAVDSD 206

B-box zinc finger;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1351339760  77 KAQCCDKHDSELLTFYCEEDDTVACRDCILETHSKHDFKKI 117
Cdd:pfam00643   2 KERLCPEHEEEPLTLYCNDCQELLCEECSVGEHRGHTVVPL 42

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760  69 EQLRHILDKAQCCD---KHDSELLTFYCEE-------DDTVACRDCILETHSKHDfKKIGDVVKVQREL--IQAKFKCLT 136
Cdd:pfam05701  80 EELKLNLERAQTEEaqaKQDSELAKLRVEEmeqgiadEASVAAKAQLEVAKARHA-AAVAELKSVKEELesLRKEYASLV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 137 TEKLTRFEKAEKVIM---ETEDEVTE-----NQTK-VLRL-------VDSQKL--AMTKEINKNskTFKREIKdyyqQVE 198
Cdd:pfam05701 159 SERDIAIKRAEEAVSaskEIEKTVEEltielIATKeSLESahaahleAEEHRIgaALAREQDKL--NWEKELK----QAE 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 199 KDVRQQTDAYL--TSVKQHLETYETKIQS------DYTEMKrfINDKSREITTEVKALTSTQMKTLEAKKDKQEMnKISI 270
Cdd:pfam05701 233 EELQRLNQQLLsaKDLKSKLETASALLLDlkaelaAYMESK--LKEEADGEGNEKKTSTSIQAALASAKKELEEV-KANI 309

                         250
                  ....*....|.
gi 1351339760 271 QSIRDFAQQLT 281
Cdd:pfam05701 310 EKAKDEVNCLR 320

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760  171 QKLAMTKEINKNSKtFKREIKDYYQQVEKDVRQqtdayltsVKQHLETYETKIQSDYTEMKRFINDKSREITTEVKALTS 250
Cdd:smart00502   1 QREALEELLTKLRK-KAAELEDALKQLISIIQE--------VEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKE 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1351339760  251 TQMKTLEAKKDKQEMNKISIQSIRDFAQQLTDTGSDIEVMAHSKKLQTRIQELE 304
Cdd:smart00502  72 NKLKVLEQQLESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLL 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTK 539
Cdd:cd05819   115 IYVADTGNHRIQKFDPDGEFLTTFGS---GGSGPGQFNGPTGVAVDSDGNIYVADTGNHRIQVFDPDGNFLttfGSTGTG 191

                          90
                  ....*....|....*
gi 1351339760 540 SDNIELPISVAVNSN 554
Cdd:cd05819   192 PGQFNYPTGIAVDSD 206

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTK-SD 541
Cdd:cd05819    68 LYVADTGNHRIQKFDPDGNFLASFGG---SGDGDGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGSGgSG 144

                          90       100
                  ....*....|....*....|
gi 1351339760 542 NIEL--PISVAVNSNWELVV 559
Cdd:cd05819   145 PGQFngPTGVAVDSDGNIYV 164

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTRGQsggGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTKSD- 541
Cdd:cd14954    84 IIVADKDNHRIQVFDLNGRFLLKFGERGT---KNGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAg 160

                          90       100
                  ....*....|....*....|
gi 1351339760 542 --NIELPISVAVNSNWELVV 559
Cdd:cd14954   161 pgQLDSPRGVAVNPDGNIVV 180

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVviFQYgTRGQSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTK 539
Cdd:cd14957   172 IYVADTGNHRIQVFTSSGT--FQY-TFGSSGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSGAYQysiGTSGSG 248

                          90
                  ....*....|....*
gi 1351339760 540 SDNIELPISVAVNSN 554
Cdd:cd14957   249 NGQFNYPYGIAVDND 263

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 461 NAIIVSDYWAHCVYAVTPQGVVIFQYGTRGQsggGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTKS 540
Cdd:cd14960   164 NEIIVTDFHNHSVKVFNAEGEFLFKFGSNGE---GNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1351339760 541 DNIELPISVAVNSNWELVVGTAGGE-ISAYKY 571
Cdd:cd14960   241 DPLYGPQGLALTSDGHVVVADSGNHcFKVYRY 272

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 474 YAVTPQGVVIFQYGTRGQsggGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTKSDNIELPISVA 550
Cdd:cd14954     1 RDYRAKGRPLLSFGKEGS---KDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLrkfGSYGSRDGQFDRPAGVA 77

                  ....*....
gi 1351339760 551 VNSNWELVV 559
Cdd:cd14954    78 VNSRGRIIV 86

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 493 GGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTK-SDNIEL--PISVAVNSNWELVV 559
Cdd:cd05819     1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSFGSFgSGDGQFnePAGVAVDSDGNLYV 70

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 397 LRDIQCTDDGCILAVHDDFSCGKtgsVFSSTGQCnreISRV-VKARIPIPMCSGVLlrCAYHHGINaIIVSDYWAHCVYA 475
Cdd:cd14960    19 LQGVAASSSGRLVIADSNNQCVQ---VFSNDGQF---KLRFgVRGRSPGQLQRPTG--VAVTLNGD-IIIADYDNKWVSI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 476 VTPQGVVIFQYGTrgqsgggdGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTKSDNIELPISVAVN 552
Cdd:cd14960    90 FSPDGKFKSKIGA--------GKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVtrfGSRGNGDRQFAGPHFAAVN 161

                  ....*..
gi 1351339760 553 SNWELVV 559
Cdd:cd14960   162 NNNEIIV 168

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVV-IFQYGTRGQSGGGDG----QLWNPGAVCVDTFGHIFIADRDNDRV 523
Cdd:cd14953   255 LYVADSGNHRIRKITPAGVVtTVAGGGAGFSGDGGPatsaQFNNPTGVAVDAAGNLYVADTGNNRI 320

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVV--IFQYGTRGQSGGGDG---QLWNPGAVCVDTFGHIFIADRDNDRV 523
Cdd:cd14953    90 LYVADTGNHRIRKITPDGVVstLAGTGTAGFSDDGGAtaaQFNYPTGVAVDAAGNLYVADTGNHRI 155

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 465 VSDYWAHCVYAVTPQGVVIFQYGTRGqsgGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTKSDNI- 543
Cdd:cd14956   169 VADTYNDRIQVFDNDGAFLRKWGGRG---TGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPg 245

                          90
                  ....*....|....*...
gi 1351339760 544 --ELPISVAVNSNWELVV 559
Cdd:cd14956   246 qfKNPWGVVVDADGTVYV 263

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrGQSG--GGDG---QLWNPGAVCVDTFGHIFIADRDNDRV 523
Cdd:cd14953    36 LYVADRGNHRIRKITPDGVVTTVAGT-GTAGfaDGGGaaaQFNTPSGVAVDAAGNLYVADTGNHRI 100

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTRGQSGGGDG-----QLWNPGAVCVDTFGHIFIADRDNDRV 523
Cdd:cd14953   145 LYVADTGNHRIRKITPDGVVTTVAGTGGAGYAGDGpataaQFNNPTGVAVDAAGNLYVADRGNHRI 210

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVL 526
Cdd:cd14956   214 VFVADFGNNRIQKFTADGTFLTSWGS---PGTGPGQFKNPWGVVVDADGTVYVADSNNNRVQRF 274

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTRGQsggGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVL 526
Cdd:cd14963   208 LYVVDNLSHRVYVFDEQGKELFTFGGRGK---DDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 465 VSDYWAHCVYAVTPQGVVIFQYGTRGQsggGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNILTKSDNIE 544
Cdd:cd14963   116 VSDVKKHKVIVFDLEGKLLLEFGKPGS---EPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKELNGSPDGKS 192

                          90       100
                  ....*....|....*....|....*....
gi 1351339760 545 ---LPISVAVNSNWEL-VVGTAGGEISAY 569
Cdd:cd14963   193 gfvNPRGIAVDPDGNLyVVDNLSHRVYVF 221

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFlgniLTK--- 539
Cdd:cd14955   123 VYVTDSGNNRIQKFDSSGTFITKWGS---FGSGDGQFNSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTF----LTKwgs 195

                          90
                  ....*....|....*...
gi 1351339760 540 --SDNIEL--PISVAVNS 553
Cdd:cd14955   196 egSGDGQFnaPYGIAVDS 213

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 403 TDDGCILAVHDdfscGKTG-SVFSSTGQCNREISRVVKARIPIPMCSGVLLRCAYHhginaIIVSDYWAHCVYAVTPQGv 481
Cdd:cd14961    19 TPTGRVVVADD----GNKRiQVFDSDGNCLQQFGPKGDAGQDIRYPLDVAVTPDGH-----IVVTDAGDRSVKVFSFDG- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 482 vifqygtRGQSGGGDGQLwNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRF--LGNILTKSDNIELPISVAVNSNWELVV 559
Cdd:cd14961    89 -------RLKLFVRKSFS-LPWGVAVNPSGEILVTDSEAGKLFVLTVDFKLgiLKKGQKLCSQLCRPRFVAVSRLGAVAV 160

B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1351339760  80 CCDKHDSELLTFYCEEDDTVACRDCILETHSKHDFKKIGDVV 121
Cdd:cd19796     3 YCEIHEHEVLRLYCDTCSVPICRECTMGEHRGHSFIYLQEAV 44

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 463 IIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFL---GNILTK 539
Cdd:cd14957    78 IYVADTDNNRIQVFNSSGVYQYSIGT---GGSGDGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTSSGTFSysiGSGGTG 154

                          90
                  ....*....|....*
gi 1351339760 540 SDNIELPISVAVNSN 554
Cdd:cd14957   155 PGQFNGPQGIAVDSD 169

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351339760 382 LDKPeRNVCFNVRG--WLRDiqcTDDGCILAVHDDfscGKTGSVFSSTGQCNREISRvvkaripiPmcSGVllrCAYHHG 459
Cdd:cd14954   164 LDSP-RGVAVNPDGniVVSD---FNNHRLQVFDPD---GQFLRFFGSEGSGNGQFKR--------P--RGV---AVDDEG 223

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 460 inAIIVSDYWAHCVYAVTPQGVVIFQYGTrgqSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVV 525
Cdd:cd14954   224 --NIIVADSGNHRVQVFSPDGEFLCSFGT---EGNGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQV 284

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351339760 484 FQYGTrGQSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRF---LGNILTKSDNIELPISVAVNSN 554
Cdd:cd14957     3 FSYAF-GSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYsysIGSGGTGSGQFNSPYGIAVDSN 75

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1351339760  81 CDKHDSELLTFYCEEDDTVACRDCILETHSKH 112
Cdd:cd19759     4 CPNHDGETLEFYCESCETAVCRECTAGEHNEH 35

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351339760 490 GQSGGGDGQLWNPGAVCVDTFGHIFIADRDNDRVVVLGLEGRFLGNI---LTKSDNIELPISVAVN 552
Cdd:cd14959    12 GESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQVFDKEGEFKFQFgipGKRDGQLWYPNKVAVC 77

B-box-type 2 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar proteins; TRIM66, also termed transcriptional intermediary factor 1 delta (TIF1delta), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor 1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TRIM66 displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TRIM66 plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TRIM66 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1351339760  80 CCDKHDSELLTFYCEEDDTVACRDCILETHSKHDFKKIGDV 120
Cdd:cd19794     2 MCPLHNQEPLKLFCETCDVLVCRSCLLSEHKEHRFKHLDEA 42