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Conserved domains on  [gi|1835671274|ref|XP_033806530|]
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tripartite motif-containing protein 3 isoform X3 [Geotrypetes seraphini]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 446-762 0e+00

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: 550.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 446 ELIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQCiqslfsadefdsmavqrstvtsswnqwdkslsqnerqygVQ 525
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQC---------------------------------------VQ 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 526 VFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIV 605
Cdd:cd14960    42 VFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIADYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIV 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 606 VDNKACCVFIFQCNGKLVSRFGSRGVADRQFAGtldgPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNG 685
Cdd:cd14960   122 VDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAG----PHFAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNG 197

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835671274 686 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVYRYLQ 762
Cdd:cd14960   198 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 136-256 2.66e-33

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


:

Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 124.19  E-value: 2.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 136 HKTSLKNQLDAIKSRLPQLSSAILRVTDISQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKVLQTQ 215
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1835671274 216 LDCLLQGQENIQSSCSFTEQALDHGTETEVLLVKKQMCDRL 256
Cdd:cd20482    81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARL 121
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 86-131 1.59e-29

B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 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, 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.


:

Pssm-ID: 380883 [Multi-domain]  Cd Length: 47  Bit Score: 110.87  E-value: 1.59e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274  86 VTGKPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKD 131
Cdd:cd19825     2 VAGKPLSCPNHEGKTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 300-399 1.03e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


:

Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  300 AHETVVTGEGLRHALVGQQTSVTITTKDKegelvksGNALIQAEITAPDGGFVEGEVLDNKNGTYELLYTLRQEGDFQLS 379
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73

                           90       100
                   ....*....|....*....|
gi 1835671274  380 IRLYDQPLRGSPFRVRAVKP 399
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVGPA 93
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 21-40 3.35e-08

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16768:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 48  Bit Score: 50.39  E-value: 3.35e-08
                          10        20
                  ....*....|....*....|
gi 1835671274  21 RCLHNYIPPQSLTLSCPVCR 40
Cdd:cd16768    29 RCLQNYIPPQSLTLSCPVCR 48
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 446-762 0e+00

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: 550.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 446 ELIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQCiqslfsadefdsmavqrstvtsswnqwdkslsqnerqygVQ 525
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQC---------------------------------------VQ 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 526 VFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIV 605
Cdd:cd14960    42 VFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIADYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIV 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 606 VDNKACCVFIFQCNGKLVSRFGSRGVADRQFAGtldgPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNG 685
Cdd:cd14960   122 VDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAG----PHFAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNG 197

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835671274 686 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVYRYLQ 762
Cdd:cd14960   198 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 136-256 2.66e-33

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 124.19  E-value: 2.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 136 HKTSLKNQLDAIKSRLPQLSSAILRVTDISQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKVLQTQ 215
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1835671274 216 LDCLLQGQENIQSSCSFTEQALDHGTETEVLLVKKQMCDRL 256
Cdd:cd20482    81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARL 121
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 86-131 1.59e-29

B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 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, 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.


Pssm-ID: 380883 [Multi-domain]  Cd Length: 47  Bit Score: 110.87  E-value: 1.59e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274  86 VTGKPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKD 131
Cdd:cd19825     2 VAGKPLSCPNHEGKTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
539-760 1.07e-27

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 113.19  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 539 VRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSP-EGKFKNKIGAGRLMGPKGVAIDRNGHIIVVDNkaccvfifq 617
Cdd:COG4257    50 FTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPkTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQ--------- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 618 cNGKLVSRF--GSRGVADRQFAGTLDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFgshgEGNGQFNAPTGVAV 695
Cdd:COG4257   121 -GGNRIGRLdpATGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAV 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835671274 696 DSNGNIIVADWGNSRIQVFD-SSGSFLSYinTMADPLYGPQGLALTSDGHVIVADSGNHcfKVYRY 760
Cdd:COG4257   196 DPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGARPYGVAVDGDGRVWFAESGAN--RIVRF 257
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 136-260 2.52e-27

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 107.35  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  136 HKTSLKNQLDAIKSRLPQLSSAILRVTDISQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKVLQTQ 215
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835671274  216 LDCLLQGQENIQSSCSFTEQALDHGTETEVLLVKKQMCDRLSELA 260
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLL 125
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 300-399 1.03e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  300 AHETVVTGEGLRHALVGQQTSVTITTKDKegelvksGNALIQAEITAPDGGFVEGEVLDNKNGTYELLYTLRQEGDFQLS 379
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73

                           90       100
                   ....*....|....*....|
gi 1835671274  380 IRLYDQPLRGSPFRVRAVKP 399
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVGPA 93
Filamin pfam00630
Filamin/ABP280 repeat;
297-393 1.44e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 297 SAVAHETVVTGEGLRHALVGQQTSVTITTKDKEGELvksgnaliQAEITAPDGGFVEGEVLDNKNGTYELLYTLRQEGDF 376
Cdd:pfam00630   1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDY 72

                          90
                  ....*....|....*..
gi 1835671274 377 QLSIRLYDQPLRGSPFR 393
Cdd:pfam00630  73 TVSVKFNGQHIPGSPFK 89
BBOX smart00336
B-Box-type zinc finger;
88-129 2.58e-13

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 64.67  E-value: 2.58e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835671274   88 GKPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPL 129
Cdd:smart00336   1 QRAPKCDSHGDEPAEFFCEECGALLCRTCDEAEHRGHTVVLL 42
zf-B_box pfam00643
B-box zinc finger;
89-129 3.35e-12

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 61.33  E-value: 3.35e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1835671274  89 KPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPL 129
Cdd:pfam00643   2 KERLCPEHEEEPLTLYCNDCQELLCEECSVGEHRGHTVVPL 42
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 21-40 3.35e-08

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It is encoded by the gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of the 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 C3HC4-type RING-HC 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.


Pssm-ID: 438424 [Multi-domain]  Cd Length: 48  Bit Score: 50.39  E-value: 3.35e-08
                          10        20
                  ....*....|....*....|
gi 1835671274  21 RCLHNYIPPQSLTLSCPVCR 40
Cdd:cd16768    29 RCLQNYIPPQSLTLSCPVCR 48
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 687-714 2.11e-07

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: 47.40  E-value: 2.11e-07
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVF 714
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 672-761 1.54e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 51.78  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  672 EFLFKFGSH-GEG-NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI-----------NTMADPLYGPQGLA 738
Cdd:PLN02919   786 DNLFKFGDHdGVGsEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPATKRVTTLagtgkagfkdgKALKAQLSEPAGLA 865

                           90       100
                   ....*....|....*....|...
gi 1835671274  739 LTSDGHVIVADSGNhcfKVYRYL 761
Cdd:PLN02919   866 LGENGRLFVADTNN---SLIRYL 885
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
 687-748 1.32e-03

ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin biosynthesis and export, and its paralog ScyD. Some members of the family contain a C-terminal PEP-CTERM domain that predictions anchoring to the outer membrane.


Pssm-ID: 467996 [Multi-domain]  Cd Length: 330  Bit Score: 41.49  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSfLSYI------NTMADPLYGPQGLALTSDGHVIVA 748
Cdd:NF033206  249 FTGLTDLAFDPDGNLYVLELAGGGLLKGDPTGS-LIRIapdgtrTTLLDGLELPTGLAVGPDGTLYVT 315
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-264 8.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 139 SLKNQLDAIKSRLPQLSSAILRVtdisQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKvLQTQLDC 218
Cdd:COG4717   136 ALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAE 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274 219 LLQGQENIQSSCSFTEQALDhgtETEVLLVKKQMCDRLSELASRAF 264
Cdd:COG4717   211 LEEELEEAQEELEELEEELE---QLENELEAAALEERLKEARLLLL 253
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
 446-762 0e+00

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: 550.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 446 ELIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQCiqslfsadefdsmavqrstvtsswnqwdkslsqnerqygVQ 525
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQC---------------------------------------VQ 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 526 VFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIV 605
Cdd:cd14960    42 VFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIADYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIV 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 606 VDNKACCVFIFQCNGKLVSRFGSRGVADRQFAGtldgPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNG 685
Cdd:cd14960   122 VDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAG----PHFAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNG 197

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835671274 686 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVYRYLQ 762
Cdd:cd14960   198 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 455-758 1.33e-84

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: 269.19  E-value: 1.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 455 GREKGEFTNLQGISASGNNRIVAADSNNQCIQslfsadefdsmavqrstvtsswnqwdkslsqnerqygvqVFSSEGQFK 534
Cdd:cd05819     1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQ---------------------------------------VFDPDGNFI 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 535 LRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIG-----AGRLMGPKGVAIDRNGHIIVVDNK 609
Cdd:cd05819    42 TSFGSFGSGDGQFNEPAGVAVDSDGNLYVADTGNHRIQKFDPDGNFLASFGgsgdgDGEFNGPRGIAVDSSGNIYVADTG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 610 ACCVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNA 689
Cdd:cd05819   122 NHRIQKFDPDGEFLTTFGSGGSGPGQF----NGPTGVAVDSDGNIYVADTGNHRIQVFDPDGNFLTTFGSTGTGPGQFNY 197

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835671274 690 PTGVAVDSNGNIIVADWGNSRIQVFDSSGSFL----SYINTmADPLYGPQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:cd05819   198 PTGIAVDSDGNIYVADSGNNRVQVFDPDGAGFggngNFLGS-DGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 447-758 1.49e-84

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: 269.80  E-value: 1.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 447 LIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQciqslfsadefdsmavqrstvtsswnqwdkslsqneRqygVQV 526
Cdd:cd14954     9 PLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNN------------------------------------R---VQV 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 527 FSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIG-----AGRLMGPKGVAIDRNG 601
Cdd:cd14954    50 FDPDGKFLRKFGSYGSRDGQFDRPAGVAVNSRGRIIVADKDNHRIQVFDLNGRFLLKFGergtkNGQFNYPWGVAVDSEG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 602 HIIVVDNKACCVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHG 681
Cdd:cd14954   130 RIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPGQL----DSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEG 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 682 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINT---MADPLYGPQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:cd14954   206 SGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSFGTegnGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 452-754 4.29e-67

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: 223.22  E-value: 4.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 452 GSRGREKGEFTNLQGISASGNNRIVAADSNNQCIQslfsadefdsmavqrstvtsswnqwdkslsqnerqygvqVFSSEG 531
Cdd:cd14955     6 GSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQ---------------------------------------KFDSTG 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 532 QFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNK-----IGAGRLMGPKGVAIDRNGHIIVV 606
Cdd:cd14955    47 TFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVADTGNHRIQKFDSTGTFLTKwgssgSGDGQFNSPSGIAVDSAGNVYVT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 607 DNKACCVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQ 686
Cdd:cd14955   127 DSGNNRIQKFDSSGTFITKWGSFGSGDGQF----NSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQ 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFL----SYINTmADPLYGPQGLALTSDGHVIVADSGNHC 754
Cdd:cd14955   203 FNAPYGIAVDSAGNVYVADTGNNRIQKFDSSGTFItkwgSEGSG-DGQFNSPSGIAVDSAGNVYVADSGNNR 273
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 447-759 2.76e-65

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: 218.29  E-value: 2.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 447 LIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQciqslfsadefdsmavqrstvtsswnqwdkslsqneRqygVQV 526
Cdd:cd14957     3 FSYAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNN------------------------------------R---IQV 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 527 FSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGA-----GRLMGPKGVAIDRNG 601
Cdd:cd14957    44 FTSSGVYSYSIGSGGTGSGQFNSPYGIAVDSNGNIYVADTDNNRIQVFNSSGVYQYSIGTggsgdGQFNGPYGIAVDSNG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 602 HIIVVDNKACCVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHG 681
Cdd:cd14957   124 NIYVADTGNHRIQVFTSSGTFSYSIGSGGTGPGQF----NGPQGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSG 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 682 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYG---PQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:cd14957   200 SGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSGAYQYSIGTSGSGNGQfnyPYGIAVDNDGKIYVADSNNNRIQVF 279


                  .
gi 1835671274 759 R 759
Cdd:cd14957   280 N 280
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 526-753 5.04e-64

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: 215.10  E-value: 5.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 526 VFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGA-----GRLMGPKGVAIDRN 600
Cdd:cd14954     2 DYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSygsrdGQFDRPAGVAVNSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 601 GHIIVVDNKACCVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSH 680
Cdd:cd14954    82 GRIIVADKDNHRIQVFDLNGRFLLKFGERGTKNGQF----NYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFE 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835671274 681 GEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMAD---PLYGPQGLALTSDGHVIVADSGNH 753
Cdd:cd14954   158 GAGPGQLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSgngQFKRPRGVAVDDEGNIIVADSGNH 233
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 452-753 2.32e-62

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: 210.22  E-value: 2.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 452 GSRGREKGEFTNLQGISASGNNRIVAADSNNQCIQslfsadefdsmavqrstvtsswnqwdkslsqnerqygvqVFSSEG 531
Cdd:cd14956     3 GGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQ---------------------------------------VFDKDG 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 532 QFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIG-----AGRLMGPKGVAIDRNGHIIVV 606
Cdd:cd14956    44 TFLRRFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDRIQVFTLTGELQTIGGssgsgPGQFNAPRGVAVDADGNLYVA 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 607 DNKACCVFIFQCNGKLVSRFGSRGVAdrqfAGTLDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQ 686
Cdd:cd14956   124 DFGNQRIQKFDPDGSFLRQWGGTGIE----PGSFNYPRGVAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQ 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMAD---PLYGPQGLALTSDGHVIVADSGNH 753
Cdd:cd14956   200 FNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTgpgQFKNPWGVVVDADGTVYVADSNNN 269
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 537-753 4.04e-55

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: 190.87  E-value: 4.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 537 FGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIG-----AGRLMGPKGVAIDRNGHIIVVDNKAC 611
Cdd:cd14955     5 WGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGssgsgDGQFYSPTGIAVDSDGNVYVADTGNH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 612 CVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPT 691
Cdd:cd14955    85 RIQKFDSTGTFLTKWGSSGSGDGQF----NSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQFNSPT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835671274 692 GVAVDSNGNIIVADWGNSRIQVFDSSGSFL----SYiNTMADPLYGPQGLALTSDGHVIVADSGNH 753
Cdd:cd14955   161 GIAVDSAGNVYVADTGNNRIQKFTSTGTFLtkwgSE-GSGDGQFNAPYGIAVDSAGNVYVADTGNN 225
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 452-759 4.46e-53

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: 185.17  E-value: 4.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 452 GSRGREKGEFTNLQGISASGNNRIVAADSNNQciqslfsadefdsmavqrstvtsswnqwdkslsqneRqygVQVFSSEG 531
Cdd:cd14961     1 GSFGGWPGTLNNPTGVAVTPTGRVVVADDGNK------------------------------------R---IQVFDSDG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 532 QFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGaGRLMGPKGVAIDRNGHIIVVDNKAC 611
Cdd:cd14961    42 NCLQQFGPKGDAGQDIRYPLDVAVTPDGHIVVTDAGDRSVKVFSFDGRLKLFVR-KSFSLPWGVAVNPSGEILVTDSEAG 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 612 CVFIFQCNGKLVSRFGSRGVAdrqfaGTLDGPHFVAVNNKNEIVVTD--------FHNHSVKVYSADGEFLFKFGS--HG 681
Cdd:cd14961   121 KLFVLTVDFKLGILKKGQKLC-----SQLCRPRFVAVSRLGAVAVTEhlfangtrSSSTRVKVFSSGGQLLGQIDSfgLN 195

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835671274 682 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVYR 759
Cdd:cd14961   196 LVFPSLICASGVAFDSEGNVIVADTGSGAILCLGKPEGFPILKPIVTQGLSRPVGLAVTPDGSLVVLDSGNHCVKIYK 273
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 504-758 2.94e-51

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: 179.79  E-value: 2.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 504 VTSSWNQWDKSLSQNERqygVQVFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNK 583
Cdd:cd14963    15 VAVSDGRIYVADTNNHR---VQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 584 IGAGR----LMGPKGVAIDRnGHIIVVDNKACCVFIFQCNGKLVSRFGSRGvadrQFAGTLDGPHFVAVNNKNEIVVTDF 659
Cdd:cd14963    92 FPEKKdrvkLISPAGLAIDD-GKLYVSDVKKHKVIVFDLEGKLLLEFGKPG----SEPGELSYPNGIAVDEDGNIYVADS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 660 HNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMAD---PLYGPQG 736
Cdd:cd14963   167 GNGRIQVFDKNGKFIKELNGSPDGKSGFVNPRGIAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKddgQFNLPNG 246

                         250       260
                  ....*....|....*....|..
gi 1835671274 737 LALTSDGHVIVADSGNHCFKVY 758
Cdd:cd14963   247 LFIDDDGRLYVTDRENNRVAVY 268
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 537-759 7.18e-51

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: 179.02  E-value: 7.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 537 FGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGA-----GRLMGPKGVAIDRNGHIIVVDNKAC 611
Cdd:cd14956     2 WGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTtgdgpGQFGRPRGLAVDKDGWLYVADYWGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 612 CVFIFQCNGKLVSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPT 691
Cdd:cd14956    82 RIQVFTLTGELQTIGGSSGSGPGQF----NAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIEPGSFNYPR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835671274 692 GVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTmadPLYG------PQGLALTSDGHVIVADSGNHCFKVYR 759
Cdd:cd14956   158 GVAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGG---RGTGpgqfnyPYGIAIDPDGNVFVADFGNNRIQKFT 228
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 523-761 6.27e-50

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: 176.24  E-value: 6.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 523 GVQVFSsEGQFKLRFgVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMG-PKGVAID-RN 600
Cdd:cd14962    34 AVFVFD-LPNGKVFV-IGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRAIGAGALFKrPTGIAVDpAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 601 GHIIVVDNKACCVFIFQCNGKLVSRFGSRGVADRQFAGtldgPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSH 680
Cdd:cd14962   112 KRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNL----PTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGER 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 681 GEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI-NTMADP--LYGPQGLALTSDGHVIVADSGNHCFKV 757
Cdd:cd14962   188 GDGPGSFARPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVgGPGSGPgeFYLPSGIAIDKDDRIYVVDQFNRRIQV 267


                  ....
gi 1835671274 758 YRYL 761
Cdd:cd14962   268 FQYL 271
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 547-758 2.94e-45

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: 163.14  E-value: 2.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 547 LQRPTGVTVDKNGDIIVADYDNRWVSIFS-PEGKFK--NKIGAGRLMGPKGVAIDRNGHIIVVDNKACCVFIFQCNGKLV 623
Cdd:cd14962    11 LTRPYGVAADGRGRIYVADTGRGAVFVFDlPNGKVFviGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 624 SRFGSRGVADRqfagtldgPHFVAVNNKN-EIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNII 702
Cdd:cd14962    91 RAIGAGALFKR--------PTGIAVDPAGkRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNLPTDLAVDRDGNLY 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 703 VADWGNSRIQVFDSSGSFLSYINTMADPlYG----PQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:cd14962   163 VTDTMNFRVQIFDADGKFLRSFGERGDG-PGsfarPKGIAVDSEGNIYVVDAAFDNVQIF 221
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
 446-761 2.34e-43

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: 158.20  E-value: 2.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 446 ELIFR--VGSRGREKGEFTNLQGISASGNNRIVAADSNNQCIQslfsadefdsmavqrstvtsswnqwdkslsqnerqyg 523
Cdd:cd14959     4 KMIIHckFGESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQ------------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 524 vqVFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKN-GDIIVADYDN--RWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRN 600
Cdd:cd14959    47 --VFDKEGEFKFQFGIPGKRDGQLWYPNKVAVCRVtGRYVVTDRGNprHRMQIFTKRGQFVRKFGARYLQHVRGLTVDAA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 601 GHIIVVDNKACCVFIFQCNGKLVSRFGSrgvadrqfAGTLDGPHFVAVNNkNEIVVTDFHNHSVKVYSADGEFLFKFGsh 680
Cdd:cd14959   125 GHIIVVESKVMRVFIFDESGNVLKWFDC--------SKYLEEPSDVAVND-NEIYICDNKGHCVVVFNYDGQFLRRIG-- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 681 geGNGQFNAPTGVAVDSNGNIIVADWGNSR--IQVFDSSGSFLSYINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:cd14959   194 --GEGITNYPIGVDISSAGDVLVADNHGNHfhVTVFTRDGQLISEFECPRVKHSRCCGLALTSEGSIVTLSKHNHHVLVF 271


                  ...
gi 1835671274 759 RYL 761
Cdd:cd14959   272 NTL 274
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
 544-752 2.17e-36

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: 138.94  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 544 PGQLQRPTGVTVDKNGD-IIVADYDNRWVS--------------------IFSPEGKFKNKIGAGRLMGPKGVAIDRNGH 602
Cdd:cd14958     9 SLKLGQVSGVAVDSLGNgVVFHRGGRVWDAnsfdanvyvfkgpieedtilVFDPDGGFLRSWGAGLFYMPHGLTIDPDGN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 603 IIVVDNKACCVFIFQCNGKLVSR--FGSRGVADRqfagtlDGPHF-----VAVNNKNEIVVTDFH-NHSVKVYSADGEFL 674
Cdd:cd14958    89 IWVTDVGLHQVFKFDPEGKLLPLltLGERGEPGS------DQTHFckptdVAVAPDGDIFVADGYcNSRIVKFSPDGKLL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835671274 675 FKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLS-YINTMADPLYgpqGLALTSDGHVIVADSGN 752
Cdd:cd14958   163 KSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLTeWTNPELGRPY---ALAIDPDGLLYVVDGPP 238
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 623-754 1.29e-35

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: 136.17  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 623 VSRFGSRGVADRQFagtlDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNII 702
Cdd:cd14955     2 VTQWGSYGSGDGQF----NSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835671274 703 VADWGNSRIQVFDSSGSFL----SYiNTMADPLYGPQGLALTSDGHVIVADSGNHC 754
Cdd:cd14955    78 VADTGNHRIQKFDSTGTFLtkwgSS-GSGDGQFNSPSGIAVDSAGNVYVTDSGNNR 132
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 136-256 2.66e-33

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 124.19  E-value: 2.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 136 HKTSLKNQLDAIKSRLPQLSSAILRVTDISQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKVLQTQ 215
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1835671274 216 LDCLLQGQENIQSSCSFTEQALDHGTETEVLLVKKQMCDRL 256
Cdd:cd20482    81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARL 121
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 538-753 3.18e-32

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: 127.65  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 538 GVRGRSPG-----QLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEG-----------KFKNKIGA--GRLMGPKGVAIDR 599
Cdd:cd14953    62 GTAGFADGggaaaQFNTPSGVAVDAAGNLYVADTGNHRIRKITPDGvvstlagtgtaGFSDDGGAtaAQFNYPTGVAVDA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 600 NGHIIVVDNKACCVFIFQCNGKlVSRFGSRGVADRQFAGT-----LDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFL 674
Cdd:cd14953   142 AGNLYVADTGNHRIRKITPDGV-VTTVAGTGGAGYAGDGPataaqFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVT 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 675 FKFGSHGEG--------NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGsflsYINTMAD---------------PL 731
Cdd:cd14953   221 TVAGTGTAGfsgdggatAAQLNNPTGVAVDAAGNLYVADSGNHRIRKITPAG----VVTTVAGggagfsgdggpatsaQF 296

                         250       260
                  ....*....|....*....|..
gi 1835671274 732 YGPQGLALTSDGHVIVADSGNH 753
Cdd:cd14953   297 NNPTGVAVDAAGNLYVADTGNN 318
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 546-754 1.08e-31

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: 126.11  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 546 QLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGK-----------FKNKIG-AGRLMGPKGVAIDRNGHIIVVDNKACCV 613
Cdd:cd14953    21 RFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVvttvagtgtagFADGGGaAAQFNTPSGVAVDAAGNLYVADTGNHRI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 614 FIFQCNGkLVSRFGSRGVADRQFAGT-----LDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEF-----LFKFGSHGEG 683
Cdd:cd14953   101 RKITPDG-VVSTLAGTGTAGFSDDGGataaqFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVttvagTGGAGYAGDG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 684 NG---QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSflsyINTMA---------DP------LYGPQGLALTSDGHV 745
Cdd:cd14953   180 PAtaaQFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGV----VTTVAgtgtagfsgDGgataaqLNNPTGVAVDAAGNL 255


                  ....*....
gi 1835671274 746 IVADSGNHC 754
Cdd:cd14953   256 YVADSGNHR 264
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 86-131 1.59e-29

B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 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, 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.


Pssm-ID: 380883 [Multi-domain]  Cd Length: 47  Bit Score: 110.87  E-value: 1.59e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274  86 VTGKPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKD 131
Cdd:cd19825     2 VAGKPLSCPNHEGKTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 636-758 1.48e-28

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: 115.47  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 636 FAGTLDGPHFVAVNNKNeIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 715
Cdd:cd14963     5 FGDPLNKPMGVAVSDGR-IYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1835671274 716 SSGSFLSYIntmADP-----LYGPQGLALtSDGHVIVADSGNHCFKVY 758
Cdd:cd14963    84 PDGKFLKYF---PEKkdrvkLISPAGLAI-DDGKLYVSDVKKHKVIVF 127
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
539-760 1.07e-27

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 113.19  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 539 VRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSP-EGKFKNKIGAGRLMGPKGVAIDRNGHIIVVDNkaccvfifq 617
Cdd:COG4257    50 FTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPkTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQ--------- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 618 cNGKLVSRF--GSRGVADRQFAGTLDGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFgshgEGNGQFNAPTGVAV 695
Cdd:COG4257   121 -GGNRIGRLdpATGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAV 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835671274 696 DSNGNIIVADWGNSRIQVFD-SSGSFLSYinTMADPLYGPQGLALTSDGHVIVADSGNHcfKVYRY 760
Cdd:COG4257   196 DPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGARPYGVAVDGDGRVWFAESGAN--RIVRF 257
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 136-260 2.52e-27

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 107.35  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  136 HKTSLKNQLDAIKSRLPQLSSAILRVTDISQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKVLQTQ 215
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835671274  216 LDCLLQGQENIQSSCSFTEQALDHGTETEVLLVKKQMCDRLSELA 260
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLL 125
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
544-760 1.05e-24

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 104.33  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 544 PGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPE-GKFKnKIGAGRLMGPKGVAIDRNGHIIVVDNKACCVFIFQCNGKL 622
Cdd:COG4257    13 PAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPAtGEFT-EYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 623 VSRFGsrgvadrqFAGTLDGPHFVAVNNKNEIVVTDFHNHSV-KVYSADGEFLFKFGSHGEGNgqfnaPTGVAVDSNGNI 701
Cdd:COG4257    92 ITTFA--------LPGGGSNPHGIAFDPDGNLWFTDQGGNRIgRLDPATGEVTEFPLPTGGAG-----PYGIAVDPDGNL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835671274 702 IVADWGNSRIQVFDSSGSFLSYInTMADPLYGPQGLALTSDGHVIVADSGNHcfKVYRY 760
Cdd:COG4257   159 WVTDFGANAIGRIDPDTGTLTEY-ALPTPGAGPRGLAVDPDGNLWVADTGSG--RIGRF 214
Bbox2_TRIM2_C-VII cd19824
B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar ...
 90-131 7.25e-24

B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) 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. TRIM2 also plays a role in mediating the p42/p44 Semi-independent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Aim) in rapid ischemic tolerance. TRIM2 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, 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.


Pssm-ID: 380882 [Multi-domain]  Cd Length: 42  Bit Score: 94.74  E-value: 7.25e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1835671274  90 PLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKD 131
Cdd:cd19824     1 PLSCPNHDGNVMEFYCQSCETAMCQECTEGEHAEHPTVPLKD 42
Bbox2_TRIM2-like cd19759
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and ...
 90-131 2.74e-23

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.


Pssm-ID: 380817 [Multi-domain]  Cd Length: 42  Bit Score: 92.89  E-value: 2.74e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1835671274  90 PLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKD 131
Cdd:cd19759     1 PLVCPNHDGETLEFYCESCETAVCRECTAGEHNEHRTVLLKD 42
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
 673-753 2.95e-23

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: 100.34  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 673 FLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLsyinTMADP-------LYGPQGLALTSDGHV 745
Cdd:cd14955     1 FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFL----TKWGSsgsgdgqFYSPTGIAVDSDGNV 76


                  ....*...
gi 1835671274 746 IVADSGNH 753
Cdd:cd14955    77 YVADTGNH 84
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 547-753 3.30e-23

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: 99.20  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 547 LQRPTGVTVDKNGDIIVADYDNRWVSifspegkfknKIGAGR----------LMGPKGVAIDRNGHIIVVDNKaccvfif 616
Cdd:cd14952    51 LYQPQGVAVDAAGTVYVTDFGNNRVL----------KLAAGSttqtvlpftgLNDPTGVAVDAAGNVYVADTG------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 617 qcNGKLVSRfgsRGVADRQ----FAGtLDGPHFVAVNNKNEIVVTDFHNHSVKVYSAdgeflfkfGSHGEGNGQF---NA 689
Cdd:cd14952   114 --NNRVLKL---AAGSNTQtvlpFTG-LSNPDGVAVDGAGNVYVTDTGNNRVLKLAA--------GSTTQTVLPFtglNS 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835671274 690 PTGVAVDSNGNIIVADWGNSRIQVFDSsGSflsyiNTMA----DPLYGPQGLALTSDGHVIVADSGNH 753
Cdd:cd14952   180 PSGVAVDTAGNVYVTDHGNNRVLKLAA-GS-----TTPTvlpfTGLNGPLGVAVDAAGNVYVADRGND 241
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
 300-399 1.03e-22

Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29).


Pssm-ID: 214720 [Multi-domain]  Cd Length: 93  Bit Score: 93.05  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  300 AHETVVTGEGLRHALVGQQTSVTITTKDKegelvksGNALIQAEITAPDGGFVEGEVLDNKNGTYELLYTLRQEGDFQLS 379
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73

                           90       100
                   ....*....|....*....|
gi 1835671274  380 IRLYDQPLRGSPFRVRAVKP 399
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVGPA 93
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
 524-715 2.87e-21

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: 95.02  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 524 VQVFSSEGQFKLRFGvrgrsPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMG----------PK 593
Cdd:cd14958    57 ILVFDPDGGFLRSWG-----AGLFYMPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEpgsdqthfckPT 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 594 GVAIDRNGHIIVVD---NKacCVFIFQCNGKLVSRFGSRGVADRQFAGtldgPHFVAVNNKNEIVVTDFHNHSVKVYSAD 670
Cdd:cd14958   132 DVAVAPDGDIFVADgycNS--RIVKFSPDGKLLKSWGEPGSGPGQFNL----PHSIALDEDGRVYVADRENGRIQVFDAD 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 671 GEFL--------------------------------------------------FKFGSHGEGNGQFNAPTGVAVDSNGN 700
Cdd:cd14958   206 GKFLtewtnpelgrpyalaidpdgllyvvdgpprlnrslpvrgfvirigkglilGRFGPGGKAPGQFQNPHDIAVDSGGD 285

                         250
                  ....*....|....*
gi 1835671274 701 IIVADWGNSRIQVFD 715
Cdd:cd14958   286 IYVGELGPNRVQKFV 300
Filamin pfam00630
Filamin/ABP280 repeat;
297-393 1.44e-20

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 86.57  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 297 SAVAHETVVTGEGLRHALVGQQTSVTITTKDKEGELvksgnaliQAEITAPDGGFVEGEVLDNKNGTYELLYTLRQEGDF 376
Cdd:pfam00630   1 AADASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDY 72

                          90
                  ....*....|....*..
gi 1835671274 377 QLSIRLYDQPLRGSPFR 393
Cdd:pfam00630  73 TVSVKFNGQHIPGSPFK 89
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 665-753 2.46e-20

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: 91.84  E-value: 2.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 665 KVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADP---LYGPQGLALTS 741
Cdd:cd14954     1 RDYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRdgqFDRPAGVAVNS 80

                          90
                  ....*....|..
gi 1835671274 742 DGHVIVADSGNH 753
Cdd:cd14954    81 RGRIIVADKDNH 92
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 538-711 1.48e-19

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: 90.28  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 538 GVRGRSPG------QLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGK------------FKNKIGAG-RLMGPKGVAID 598
Cdd:cd14953   116 GTAGFSDDggataaQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVvttvagtggagyAGDGPATAaQFNNPTGVAVD 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 599 RNGHIIVVD--N----KaccvfIFQcNGKLVSRFGSRGVADRQFAG----TLDGPHFVAVNNKNEIVVTDFHNHSVKVYS 668
Cdd:cd14953   196 AAGNLYVADrgNhrirK-----ITP-DGVVTTVAGTGTAGFSGDGGataaQLNNPTGVAVDAAGNLYVADSGNHRIRKIT 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835671274 669 ADGE----FLFKFGSHGEGNG----QFNAPTGVAVDSNGNIIVADWGNSRI 711
Cdd:cd14953   270 PAGVvttvAGGGAGFSGDGGPatsaQFNNPTGVAVDAAGNLYVADTGNNRI 320
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 676-758 2.30e-19

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: 88.88  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 676 KFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMAD---PLYGPQGLALTSDGHVIVADSGN 752
Cdd:cd14956     1 SWGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTTGDgpgQFGRPRGLAVDKDGWLYVADYWG 80


                  ....*.
gi 1835671274 753 HCFKVY 758
Cdd:cd14956    81 DRIQVF 86
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
544-723 8.10e-17

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 81.22  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 544 PGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPE-GKFKNKIGAGRLMGPKGVAIDRNGHIIVVDNKaccvfifqcNGKL 622
Cdd:COG4257    98 PGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPAtGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFG---------ANAI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 623 VsRFGSRGVADRQFAG--TLDGPHFVAVNNKNEIVVTDFHNHSVKVYS-ADGEFLfKFGSHGEGNGqfnaPTGVAVDSNG 699
Cdd:COG4257   169 G-RIDPDTGTLTEYALptPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVT-EYPLPGGGAR----PYGVAVDGDG 242

                         170       180
                  ....*....|....*....|....
gi 1835671274 700 NIIVADWGNSRIQVFDSSGSFLSY 723
Cdd:COG4257   243 RVWFAESGANRIVRFDPDTELTEY 266
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 547-711 2.82e-15

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: 76.09  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 547 LQRPTGVTVDKNGDIIVADYDNRWVSifspegkfknKIGAGR----------LMGPKGVAIDRNGHIIVVDNKACCVFif 616
Cdd:cd14952    93 LNDPTGVAVDAAGNVYVADTGNNRVL----------KLAAGSntqtvlpftgLSNPDGVAVDGAGNVYVTDTGNNRVL-- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 617 qcngKLVSrfGSRGVADRQFAGtLDGPHFVAVNNKNEIVVTDFHNHSVkvysadgeflFKF--GSHGEGNGQF---NAPT 691
Cdd:cd14952   161 ----KLAA--GSTTQTVLPFTG-LNSPSGVAVDTAGNVYVTDHGNNRV----------LKLaaGSTTPTVLPFtglNGPL 223

                         170       180
                  ....*....|....*....|
gi 1835671274 692 GVAVDSNGNIIVADWGNSRI 711
Cdd:cd14952   224 GVAVDAAGNVYVADRGNDRV 243
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 589-753 2.03e-14

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: 73.78  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 589 LMGPKGVAIDRNGHIIVVDnkaccvfifQCNGKLVS-RFGSRGVADRQFAGtLDGPHFVAVNNKNEIVVTDFHNHSVKVY 667
Cdd:cd14952     9 LDGPGGVAVDAAGNVYVAD---------SGNNRVLKlAAGSTTQTVLPFTG-LYQPQGVAVDAAGTVYVTDFGNNRVLKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 668 SAdgeflfkfGSHGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRIQVFDsSGSflsyiNTMAD-P---LYGPQGLALT 740
Cdd:cd14952    79 AA--------GSTTQTVLPFtglNDPTGVAVDAAGNVYVADTGNNRVLKLA-AGS-----NTQTVlPftgLSNPDGVAVD 144

                         170
                  ....*....|...
gi 1835671274 741 SDGHVIVADSGNH 753
Cdd:cd14952   145 GAGNVYVTDTGNN 157
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 677-754 3.97e-14

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: 74.10  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 677 FGSHGEG--NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSflsyINTMA---------DP-----LYGPQGLALT 740
Cdd:cd14953    10 AGFSGGGgtAARFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGV----VTTVAgtgtagfadGGgaaaqFNTPSGVAVD 85

                          90
                  ....*....|....
gi 1835671274 741 SDGHVIVADSGNHC 754
Cdd:cd14953    86 AAGNLYVADTGNHR 99
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
628-760 1.99e-13

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 71.20  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 628 SRGVADRQFAGTLDGPHFVAVNNKNEIVVTDFHNHSVKVYS-ADGEFlfkfgsHGEGNGQFNAPTGVAVDSNGNIIVADW 706
Cdd:COG4257     4 AVDITEYPVPAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEF------TEYPLGGGSGPHGIAVDPDGNLWFTDN 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1835671274 707 GNSRIQVFD-SSGSFLSYIntMADPLYGPQGLALTSDGHVIVADSGNHcfKVYRY 760
Cdd:COG4257    78 GNNRIGRIDpKTGEITTFA--LPGGGSNPHGIAFDPDGNLWFTDQGGN--RIGRL 128
BBOX smart00336
B-Box-type zinc finger;
88-129 2.58e-13

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 64.67  E-value: 2.58e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835671274   88 GKPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPL 129
Cdd:smart00336   1 QRAPKCDSHGDEPAEFFCEECGALLCRTCDEAEHRGHTVVLL 42
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 443-714 3.70e-13

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: 70.40  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 443 IEDELIFRVGSRGREKGEFTNLQGI----------SASGNNRIvaadsnnqciqslfsadefdsmavqrstvtsswnqwd 512
Cdd:cd14963   129 LEGKLLLEFGKPGSEPGELSYPNGIavdedgniyvADSGNGRI------------------------------------- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 513 kslsqnerqygvQVFSSEGQFKLRFgvrgrspgqlqrptgvtvdkNGDiivadydnrwvsifspegkfknKIGAGRLMGP 592
Cdd:cd14963   172 ------------QVFDKNGKFIKEL--------------------NGS----------------------PDGKSGFVNP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 593 KGVAIDRNGHIIVVDNKAccvfifqcngklvsrfgsrgvadrqfagtldgphfvavnnkneivvtdfhnHSVKVYSADGE 672
Cdd:cd14963   198 RGIAVDPDGNLYVVDNLS---------------------------------------------------HRVYVFDEQGK 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1835671274 673 FLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 714
Cdd:cd14963   227 ELFTFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 447-574 8.11e-13

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: 69.62  E-value: 8.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 447 LIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNqciqslfsadefdsmavQRstvtsswnqwdkslsqnerqygVQV 526
Cdd:cd14956   186 FLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGN-----------------NR----------------------IQK 226

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1835671274 527 FSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIF 574
Cdd:cd14956   227 FTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGTVYVADSNNNRVQRF 274
zf-B_box pfam00643
B-box zinc finger;
89-129 3.35e-12

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 61.33  E-value: 3.35e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1835671274  89 KPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPL 129
Cdd:pfam00643   2 KERLCPEHEEEPLTLYCNDCQELLCEECSVGEHRGHTVVPL 42
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
636-762 1.01e-11

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 65.49  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 636 FAGTLDGPHFVAVNNKNEIVVTDFHNHSVKVY-SADGEFL--FKFGSHgegngqfnaPTGVAVDSNGN-IIVADWGNSRI 711
Cdd:COG3391    64 AAAVADADGADAGADGRRLYVANSGSGRVSVIdLATGKVVatIPVGGG---------PRGLAVDPDGGrLYVADSGNGRV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835671274 712 QVFD-SSGSFLSYINTmadpLYGPQGLALTSDG-HVIVADSGNHcfKVYRYLQ 762
Cdd:COG3391   135 SVIDtATGKVVATIPV----GAGPHGIAVDPDGkRLYVANSGSN--TVSVIVS 181
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
538-715 1.04e-11

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 65.49  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 538 GVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPE-GKFKNKIGAGRlmGPKGVAIDRNG-HIIVVDNKACCVFI 615
Cdd:COG3391    59 GLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLAtGKVVATIPVGG--GPRGLAVDPDGgRLYVADSGNGRVSV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 616 FQC-NGKLVSRFGsrgvadrqfagTLDGPHFVAVN-NKNEIVVTDFHNHSVKVY-----SADGEFL--FKFGSHgegngq 686
Cdd:COG3391   137 IDTaTGKVVATIP-----------VGAGPHGIAVDpDGKRLYVANSGSNTVSVIvsvidTATGKVVatIPVGGG------ 199

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1835671274 687 fnaPTGVAVDSNGNIIV--------ADWGNSRIQVFD 715
Cdd:COG3391   200 ---PVGVAVSPDGRRLYvanrgsntSNGGSNTVSVID 233
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 549-721 8.65e-11

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 63.37  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 549 RPTGVTVDKNGDIIVADYDNRwVSIFSPE-GKFK---NKIGAgRLMGPKGVAIDRNGHIIVVDnkaccVFIFQCNGKLVs 624
Cdd:COG3386    50 RPNGLAFDPDGRLLVADHGRG-LVRFDPAdGEVTvlaDEYGK-PLNRPNDGVVDPDGRLYFTD-----MGEYLPTGALY- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 625 RFGSRGVAdRQFAGTLDGPHFVAVNNKNEIV-VTDFHNHSVKVY--SADGEFLFK--FGSHGEGNGqfnAPTGVAVDSNG 699
Cdd:COG3386   122 RVDPDGSL-RVLADGLTFPNGIAFSPDGRTLyVADTGAGRIYRFdlDADGTLGNRrvFADLPDGPG---GPDGLAVDADG 197

                         170       180
                  ....*....|....*....|..
gi 1835671274 700 NIIVADWGNSRIQVFDSSGSFL 721
Cdd:COG3386   198 NLWVALWGGGGVVRFDPDGELL 219
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 583-760 3.72e-10

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 61.45  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 583 KIGAGRLMGPKGVAIDRNGHIIVVDNKACCVFIFQCNGKLVSRFgsrgVADRQFAGTL----DGpHFVAVNNKNEIVVTD 658
Cdd:COG3386     1 KLADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVF----AEPSGRPNGLafdpDG-RLLVADHGRGLVRFD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 659 FHNHSVKVYsadgeflfkfgsHGEGNGQFNAPTGVAVDSNGNIIVAD----WGNSRIQVFDSSGSflsyINTMADPLYGP 734
Cdd:COG3386    76 PADGEVTVL------------ADEYGKPLNRPNDGVVDPDGRLYFTDmgeyLPTGALYRVDPDGS----LRVLADGLTFP 139

                         170       180
                  ....*....|....*....|....*..
gi 1835671274 735 QGLALTSDG-HVIVADSGNHcfKVYRY 760
Cdd:COG3386   140 NGIAFSPDGrTLYVADTGAG--RIYRF 164
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
 93-129 1.54e-09

B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2).


Pssm-ID: 380814 [Multi-domain]  Cd Length: 39  Bit Score: 53.57  E-value: 1.54e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1835671274  93 CPNHEGKMMEFYCGSCETAMCHEC-TEGEHRDHVTVPL 129
Cdd:cd19756     2 CPEHPEEPLKLFCETCQELVCVLClLSGEHRGHKVVPL 39
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 682-760 6.62e-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: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 57.60  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 682 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYG-PQGLALTSDGHVIVADSGNHcfKVYRY 760
Cdd:cd14962     6 RPKEALTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGPNRFVsPIGVAIDANGNLYVSDAELG--KVFVF 83
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 543-760 3.11e-08

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 55.67  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 543 SPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRlMGPKGVAIDRNGHIIVVDNKACCVFIFQCNGK- 621
Cdd:COG3386     3 ADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPS-GRPNGLAFDPDGRLLVADHGRGLVRFDPADGEv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 622 --LVSRFGSR------GVADRQfaGTldgphfvavnnkneIVVTDFHNH----SVKVYSADGEF--LFkfgshgegnGQF 687
Cdd:COG3386    82 tvLADEYGKPlnrpndGVVDPD--GR--------------LYFTDMGEYlptgALYRVDPDGSLrvLA---------DGL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 688 NAPTGVAVDSNGNI-IVADWGNSRIQVFD--SSGS------FLsyinTMADPLYGPQGLALTSDGHVIVADSGNHCfkVY 758
Cdd:COG3386   137 TFPNGIAFSPDGRTlYVADTGAGRIYRFDldADGTlgnrrvFA----DLPDGPGGPDGLAVDADGNLWVALWGGGG--VV 210


                  ..
gi 1835671274 759 RY 760
Cdd:COG3386   211 RF 212
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 21-40 3.35e-08

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It is encoded by the gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of the 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 C3HC4-type RING-HC 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.


Pssm-ID: 438424 [Multi-domain]  Cd Length: 48  Bit Score: 50.39  E-value: 3.35e-08
                          10        20
                  ....*....|....*....|
gi 1835671274  21 RCLHNYIPPQSLTLSCPVCR 40
Cdd:cd16768    29 RCLQNYIPPQSLTLSCPVCR 48
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
 93-137 5.58e-08

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, TRIM47 and similar proteins; This family includes a group of tripartite motif-containing proteins, such as TRIM16, TRIM29 and TRIM47. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor through affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. TRIM16 and TRIM29 belong 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. TRIM47 belongs to the C-IV subclass of TRIM family of proteins that are 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 two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) 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.


Pssm-ID: 380827 [Multi-domain]  Cd Length: 46  Bit Score: 49.63  E-value: 5.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1835671274  93 CPNHeGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDVVEQHK 137
Cdd:cd19769     3 CPIH-KKPLELFCRTDQMCICELCAKEEHRGHDVVTVEEEREKKE 46
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
 93-137 9.14e-08

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.


Pssm-ID: 380854 [Multi-domain]  Cd Length: 48  Bit Score: 48.84  E-value: 9.14e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1835671274  93 CPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDVVEQHK 137
Cdd:cd19796     4 CEIHEHEVLRLYCDTCSVPICRECTMGEHRGHSFIYLQEAVQDSK 48
Bbox2_BRAT-like cd19798
B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ...
 89-121 1.49e-07

B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380856  Cd Length: 44  Bit Score: 48.06  E-value: 1.49e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1835671274  89 KPLSCPNHEGKMMEFYCGSCETAMCHECTEGEH 121
Cdd:cd19798     2 KPVFCPKHPNEVLKFFCKTCNIPICKDCTLLDH 34
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 687-714 2.11e-07

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: 47.40  E-value: 2.11e-07
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVF 714
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
 21-40 3.13e-07

RING finger, HC subclass, 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 the 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 C3HC4-type RING-HC 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.


Pssm-ID: 438248 [Multi-domain]  Cd Length: 45  Bit Score: 47.45  E-value: 3.13e-07
                          10        20
                  ....*....|....*....|
gi 1835671274  21 RCLHNYIPPQSLTLSCPVCR 40
Cdd:cd16586    26 RCLQNYIPAESLSLSCPVCR 45
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
 646-715 1.19e-06

NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. 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: 271321 [Multi-domain]  Cd Length: 334  Bit Score: 51.42  E-value: 1.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835671274 646 VAVNNKNEIVVTDFHNHSVKVY-SADGE--FLFKFGSHGEGN--GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 715
Cdd:cd14951   201 VAALPDGSVYVADTYNHKIKRVdPATGEvsTLAGTGKAGYKDleAQFSEPSGLVVDGDGRLYVADTNNHRIRRLD 275
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
 669-753 1.50e-06

NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. 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: 271321 [Multi-domain]  Cd Length: 334  Bit Score: 51.04  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 669 ADGEFLFKFGsHGEGNGqFNA----PTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSyinTMAD-----------PLYG 733
Cdd:cd14951   175 RVGTGLFDFG-DRDGPG-AEAllqhPLGVAALPDGSVYVADTYNHKIKRVDPATGEVS---TLAGtgkagykdleaQFSE 249

                          90       100
                  ....*....|....*....|
gi 1835671274 734 PQGLALTSDGHVIVADSGNH 753
Cdd:cd14951   250 PSGLVVDGDGRLYVADTNNH 269
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 672-761 1.54e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 51.78  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  672 EFLFKFGSH-GEG-NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI-----------NTMADPLYGPQGLA 738
Cdd:PLN02919   786 DNLFKFGDHdGVGsEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPATKRVTTLagtgkagfkdgKALKAQLSEPAGLA 865

                           90       100
                   ....*....|....*....|...
gi 1835671274  739 LTSDGHVIVADSGNhcfKVYRYL 761
Cdd:PLN02919   866 LGENGRLFVADTNN---SLIRYL 885
Bbox2_TRIM56_C-V cd19789
B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar ...
 93-133 2.94e-06

B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380847  Cd Length: 47  Bit Score: 44.84  E-value: 2.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1835671274  93 CPNHEGKMMEFYCGSCETAMCHECTEGEHRD--HVTVPLKDVV 133
Cdd:cd19789     5 CREHRDERLLLYCTPCEAAVCRECRLRPHLSltHRCLPLAEAA 47
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
 21-41 2.97e-06

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); 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. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of the 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 C3HC4-type RING-HC 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.


Pssm-ID: 438423 [Multi-domain]  Cd Length: 51  Bit Score: 45.01  E-value: 2.97e-06
                          10        20
                  ....*....|....*....|.
gi 1835671274  21 RCLHNYIPPQSLTLSCPVCRQ 41
Cdd:cd16767    31 RCLQNYIPAHSLTLSCPVCRQ 51
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 731-758 5.40e-06

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: 43.54  E-value: 5.40e-06
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 731 LYGPQGLALTSDGHVIVADSGNHCFKVY 758
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Bbox2_TRIM45_C-X cd19785
B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar ...
 90-132 9.36e-06

B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of TRIM (tripartite motif) 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 region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380843  Cd Length: 43  Bit Score: 43.18  E-value: 9.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1835671274  90 PLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDV 132
Cdd:cd19785     1 PVLCPFHPAEELRLFCETCDKPVCRDCVLVEHRGHQCDFTSDV 43
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 640-667 1.29e-05

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: 42.39  E-value: 1.29e-05
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 640 LDGPHFVAVNNKNEIVVTDFHNHSVKVY 667
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 651-760 2.44e-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: 46.94  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 651 KNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVD-SNGNIIVADWGNSRIQVFD-SSGSFLSYINTMA 728
Cdd:pfam17170  53 DDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDkSNNSIYILDFMQNKILTYDlDGYSFIGEINLDL 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274 729 DP-----------LYGPQGLA--LTSDGHVIVADS-GNHCFKVYRY 760
Cdd:pfam17170 133 LPsdccqldkgklAFDSSGFDdgKRSGFYLVITDElGNIISGFFPA 178
Bbox2_TRIM67_C-I cd19827
B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 92-129 4.41e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 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.


Pssm-ID: 380885  Cd Length: 45  Bit Score: 41.51  E-value: 4.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1835671274  92 SCPNHEGKMMEFYCGSCETAMCHEC-TEGEHRDHVTVPL 129
Cdd:cd19827     2 TCAEHELENYSMYCASCRTPVCYQClEEGKHAKHEVKAL 40
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
 446-571 4.74e-05

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: 46.10  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 446 ELIFRVGSRGREKGEFTNLQGISASGNNRIVAADSNNQCIQSLFSADEFD------------SMAVQRSTVTSSWNqWDK 513
Cdd:cd14958   160 KLLKSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLtewtnpelgrpyALAIDPDGLLYVVD-GPP 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835671274 514 SLSQNERQYGVQVFSSEGQFKLRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWV 571
Cdd:cd14958   239 RLNRSLPVRGFVIRIGKGLILGRFGPGGKAPGQFQNPHDIAVDSGGDIYVGELGPNRV 296
Bbox2_TRIM66-like cd19794
B-box-type 2 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar ...
 91-132 4.99e-05

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.


Pssm-ID: 380852  Cd Length: 43  Bit Score: 41.29  E-value: 4.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1835671274  91 LSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDV 132
Cdd:cd19794     1 LMCPLHNQEPLKLFCETCDVLVCRSCLLSEHKEHRFKHLDEA 42
WD40 COG2319
WD40 repeat [General function prediction only];
535-759 7.77e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.67  E-value: 7.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 535 LRFGVRGRSPGQLQRPTGVTVDKNGDIIVADYDNRWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIVV---DNKAc 611
Cdd:COG2319    66 AAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASgsaDGTV- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 612 cvfifqcngKLVSrfgsrgVADRQFAGTLDGPHF----VAVNNKNEIVVTDFHNHSVKVYS-ADGEFLFKFGSHGegngq 686
Cdd:COG2319   145 ---------RLWD------LATGKLLRTLTGHSGavtsVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHT----- 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835671274 687 fNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLsyINTMADPLYGPQGLALTSDGHVIVADSGNHCFKVYR 759
Cdd:COG2319   205 -GAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL--LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
Bbox2_TIF1g_C-VI cd19830
B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); ...
 89-137 1.06e-04

B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); TIF1-gamma, also known as tripartite motif-containing 33 (TRIM33), ectodermin, RFG7, or PTC7, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-gamma is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling. It inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key actor of tumorigenesis. Like other TIF1 family members, TIF1-gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis.


Pssm-ID: 380888  Cd Length: 53  Bit Score: 40.43  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1835671274  89 KPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDVVEQHK 137
Cdd:cd19830     5 RPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQK 53
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 547-574 1.13e-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: 39.69  E-value: 1.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 547 LQRPTGVTVDKNGDIIVADYDNRWVSIF 574
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
YjiK COG3204
Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only];
544-743 1.52e-04

Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only];


Pssm-ID: 442437 [Multi-domain]  Cd Length: 271  Bit Score: 44.19  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 544 PGQLQRPTGVTVDKNGDIIVADYDN-RWVSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIVVDNKACCVFIFQcngkl 622
Cdd:COG3204    45 PGELDEISGLTYNPDTGTLFAVQDEpGEIFELSLTGKVLRRIPLGGFGDYEGIAYLGDGRYVLVSEGTQTLYEVT----- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 623 vsrFGSRGVADRQFAGTLDGPHFVAVNNKNEIVVTDFHNHS---VK------VYSADGEFLFKFGSHGEGNGQFNAPTGV 693
Cdd:COG3204   120 ---LDDGTTVLRADVKSLKLGLSEKGNKGFEGLAYDPKNNRlfvAKerdpdgIYEFDLDSKKLTGSPDKALKGVKDPSAL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835671274 694 AVDS-NGNIIVADWGNSRIQVFDSSGSFLSYINTMADPLYG-PQGLALTSDG 743
Cdd:COG3204   197 AIDPiTGHLLILSDESKLLLELDRDGKVVSALSLDKGFDFPqPEGIAFDPDG 248
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
467-608 1.66e-04

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.91  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 467 ISASGNNRIVAAD-SNNQCIQSLFSADEFDSMAVQRST----VTSSWNQwdkslsqnerqyGVQVFS-SEGQFKLRFGVr 540
Cdd:COG3391    84 VANSGSGRVSVIDlATGKVVATIPVGGGPRGLAVDPDGgrlyVADSGNG------------RVSVIDtATGKVVATIPV- 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835671274 541 GRSPgqlqrpTGVTVDKNGD-IIVADYDNRWVSIF-----SPEGKFKNKIGAGRlmGPKGVAIDRNGHIIVVDN 608
Cdd:COG3391   151 GAGP------HGIAVDPDGKrLYVANSGSNTVSVIvsvidTATGKVVATIPVGG--GPVGVAVSPDGRRLYVAN 216
Bbox2_TIF1a_C-VI cd19828
B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); ...
 89-124 2.10e-04

B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-alpha interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development.


Pssm-ID: 380886  Cd Length: 57  Bit Score: 39.64  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1835671274  89 KPLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDH 124
Cdd:cd19828     2 RPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEH 37
Bbox_SF cd00021
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
 93-129 3.16e-04

B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2).


Pssm-ID: 380813 [Multi-domain]  Cd Length: 39  Bit Score: 38.73  E-value: 3.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1835671274  93 CPNHEGKMMEFYCGSCETAMCHECTE-GEHRDHVTVPL 129
Cdd:cd00021     2 CQEHDEEKANKYCVTCEVLYCALCKKsGAHPDHEVAPL 39
Bbox2_TRIM37_C-VIII cd19779
B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar ...
 93-129 4.72e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as Mulibrey nanism protein, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380837  Cd Length: 40  Bit Score: 38.07  E-value: 4.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1835671274  93 CPNHEGKMmEFYCGSCETAMCHECT--EGEHRDHVTVPL 129
Cdd:cd19779     3 CETHNEKL-SVYCWTCKKCICHQCAlwGGTHSGHTFKPL 40
Bbox2_TIF1_C-VI cd19775
B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This ...
 90-124 6.56e-04

B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belong to the C-VI subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs).


Pssm-ID: 380833  Cd Length: 43  Bit Score: 38.08  E-value: 6.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1835671274  90 PLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDH 124
Cdd:cd19775     1 PLFCPVHPQEPLKLFCETCDKLTCRDCQLLEHKDH 35
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 639-715 1.00e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 42.53  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  639 TLDGPHFVAVNNKNEIVVTDFhnhsvkvysaDGEFLFKFGSHGE--------GNGQFNAPTGVAVDSNGNII-VADWGNS 709
Cdd:PLN02919   577 LLNNRLFISDSNHNRIVVTDL----------DGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKNLLyVADTENH 646


                   ....*.
gi 1835671274  710 RIQVFD 715
Cdd:PLN02919   647 ALREID 652
Bbox2_TIF1b_C-VI cd19829
B-box-type 2 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); ...
 90-133 1.13e-03

B-box-type 2 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a plant homeodomain (PHD) and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-beta acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.


Pssm-ID: 380887  Cd Length: 44  Bit Score: 37.50  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1835671274  90 PLSCPNHEGKMMEFYCGSCETAMCHECTEGEHRDHVTVPLKDVV 133
Cdd:cd19829     1 TVYCSIHKQEPLKLFCETCDTLTCRDCQLNAHKDHQYQFLEDAV 44
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
 687-748 1.32e-03

ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin biosynthesis and export, and its paralog ScyD. Some members of the family contain a C-terminal PEP-CTERM domain that predictions anchoring to the outer membrane.


Pssm-ID: 467996 [Multi-domain]  Cd Length: 330  Bit Score: 41.49  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835671274 687 FNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSfLSYI------NTMADPLYGPQGLALTSDGHVIVA 748
Cdd:NF033206  249 FTGLTDLAFDPDGNLYVLELAGGGLLKGDPTGS-LIRIapdgtrTTLLDGLELPTGLAVGPDGTLYVT 315
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
 558-734 1.38e-03

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: 41.54  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 558 NGDIIVADYDNRWVSIFSPEGKFKNKIGAgRLMGP------KGVAIDR-NGHIIVVDNKaccvfifqcNGKLVSrFGsrg 630
Cdd:pfam17170  53 DDRIFVFDSNTNNLFVFDKKGKFVRQIGA-QGNGPgeylqiNDFIIDKsNNSIYILDFM---------QNKILT-YD--- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 631 vadrqfagtLDGPHFVavnnkNEIVVTDFHNHsvkVYSADGEFLFkFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSR 710
Cdd:pfam17170 119 ---------LDGYSFI-----GEINLDLLPSD---CCQLDKGKLA-FDSSGFDDGKRSGFYLVITDELGNIISGFFPAEF 180

                         170       180
                  ....*....|....*....|....*..
gi 1835671274 711 IQ--VFDSSGSFLSYINTM-ADPLYGP 734
Cdd:pfam17170 181 TLgiLFNSSVPFYEYGDNIyFYPYYSP 207
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
 589-616 1.74e-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: 36.23  E-value: 1.74e-03
                          10        20
                  ....*....|....*....|....*...
gi 1835671274 589 LMGPKGVAIDRNGHIIVVDNKACCVFIF 616
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
 689-718 2.10e-03

SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 462480 [Multi-domain]  Cd Length: 246  Bit Score: 40.71  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1835671274 689 APTGVAVDSNGNIIVADWGNSRIQVFDSSG 718
Cdd:pfam08450 185 RPDGMAVDAEGNVWVARWGGGKVVRFDPDG 214
Bbox2_TRIM25_C-IV cd19776
B-box-type 2 zinc finger found in tripartite motif-containing protein 25 (TRIM25) and similar ...
 92-122 2.23e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 25 (TRIM25) and similar proteins; TRIM25, also termed estrogen-responsive finger protein (EFP), or ubiquitin/ISG15-conjugating enzyme TRIM25, or zinc finger protein 147 (ZNF147), or E3 ubiquitin/ISG15 ligase TRIM25, is induced by estrogen and particularly abundant in placenta and uterus. It has been implicated in cell proliferation, protein modification, and the retinoic acid inducible gene I (RIG-I)-mediated antiviral signaling pathway. It functions as an E3-ubiquitin ligase able to transfer ubiquitin and ISG15 to target proteins. It binds to mono-ubiquitinated PCNA and promotes the ISG15 modification (ISGylation) of PCNA, suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. It suppresses p53's transcriptional activity and dampens the response to DNA damage. Upon deubiquitylation by ubiquitin-specific peptidase 15 (USP15), it mediates K63-linked polyubiquitination of RIG-I that is crucial for downstream antiviral interferon signaling. TRIM25 is required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF- kappa B) and interferon production. It is an RNA binding protein acting as RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a SPRY/B30.2 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.


Pssm-ID: 380834  Cd Length: 38  Bit Score: 36.21  E-value: 2.23e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1835671274  92 SCPNHeGKMMEFYCGSCETAMCHECTEGEHR 122
Cdd:cd19776     2 KCTQH-GKLLEFYCKSHSLCICSTCLVKEHK 31
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
 547-607 2.79e-03

NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. 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: 271321 [Multi-domain]  Cd Length: 334  Bit Score: 40.64  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835671274 547 LQRPTGVTVDKNGDIIVADYDN----RW------VSIFSPEGKFKNKIGAGRLMGPKGVAIDRNGHIIVVD 607
Cdd:cd14951   195 LQHPLGVAALPDGSVYVADTYNhkikRVdpatgeVSTLAGTGKAGYKDLEAQFSEPSGLVVDGDGRLYVAD 265
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 625-715 2.86e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 41.38  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274  625 RFGSR-GVADRQFagtLDGPHFVAVNNKNEIVVTDFHNHSVKVY----------SADGEFLFKFGSHGEGngQFNAPTGV 693
Cdd:PLN02919   790 KFGDHdGVGSEVL---LQHPLGVLCAKDGQIYVADSYNHKIKKLdpatkrvttlAGTGKAGFKDGKALKA--QLSEPAGL 864

                           90       100
                   ....*....|....*....|..
gi 1835671274  694 AVDSNGNIIVADWGNSRIQVFD 715
Cdd:PLN02919   865 ALGENGRLFVADTNNSLIRYLD 886
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 91-132 2.89e-03

B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins; MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, and is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380891  Cd Length: 43  Bit Score: 36.20  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1835671274  91 LSCPNHEGKMMEFYCGSCETAMCHECTE-GEHRDHVTVPLKDV 132
Cdd:cd19833     1 LMCEEHEEEKINIYCLSCEVPTCSLCKVfGAHKDCEVAPLPTV 43
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 92-124 2.94e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif (DSGXXS) depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are 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 region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 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.


Pssm-ID: 380884  Cd Length: 49  Bit Score: 36.23  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1835671274  92 SCPNHEGKMMEFYCGSCETAMCHECTE-GEHRDH 124
Cdd:cd19826     6 TCTDHELENHSMYCVQCKMPVCYQCLEeGKHSSH 39
Bbox2_TRIM23_C-IX_rpt2 cd19774
second B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and ...
 93-131 4.07e-03

second B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and similar proteins; TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, two Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition.


Pssm-ID: 380832  Cd Length: 50  Bit Score: 35.85  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1835671274  93 CPNHEGKMMEFYCG--SCETA--MCHECTE-GEHRDHVTVPLKD 131
Cdd:cd19774     5 CPIHPDHLIEFVCLeeDCQESplMCIICKEyGKHQGHKHELLEE 48
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-264 8.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835671274 139 SLKNQLDAIKSRLPQLSSAILRVtdisQQLMERKNDAVSEISNTFEELEKALYQRKNSLIHDLEVICGAKQKvLQTQLDC 218
Cdd:COG4717   136 ALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAE 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1835671274 219 LLQGQENIQSSCSFTEQALDhgtETEVLLVKKQMCDRLSELASRAF 264
Cdd:COG4717   211 LEEELEEAQEELEELEEELE---QLENELEAAALEERLKEARLLLL 253
 
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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