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Conserved domains on  [gi|568951067|ref|XP_006508104|]
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tripartite motif-containing protein 3 isoform X2 [Mus musculus]

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; ...
373-646 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: 584.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 373 ELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVA 452
Cdd:cd14960    1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 453 DYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAV 532
Cdd:cd14960   81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 533 NNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 612
Cdd:cd14960  161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568951067 613 EPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ 646
Cdd:cd14960  241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
60-186 1.46e-38

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


:

Pssm-ID: 128778  Cd Length: 127  Bit Score: 138.55  E-value: 1.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    60 HKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQ 139
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568951067   140 LDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQ 186
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
224-321 6.23e-25

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: 98.83  E-value: 6.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   224 AHETVATGEGLRQALVGQPASLTVTTKDKdgrlvrtGSAELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLS 303
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*...
gi 568951067   304 VLLYGQPVRGSPFRVRAL 321
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVG 91
Bbox_SF super family cl00034
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
23-55 1.01e-18

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).


The actual alignment was detected with superfamily member cd19825:

Pssm-ID: 469587 [Multi-domain]  Cd Length: 47  Bit Score: 80.05  E-value: 1.01e-18
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568951067  23 KTMEFYCEACETAMCGECRAGEHREHGTVLLRD 55
Cdd:cd19825   15 KTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
373-646 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: 584.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 373 ELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVA 452
Cdd:cd14960    1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 453 DYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAV 532
Cdd:cd14960   81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 533 NNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 612
Cdd:cd14960  161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568951067 613 EPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ 646
Cdd:cd14960  241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
60-186 1.46e-38

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 138.55  E-value: 1.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    60 HKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQ 139
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568951067   140 LDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQ 186
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
60-180 2.25e-37

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: 134.97  E-value: 2.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  60 HKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQ 139
Cdd:cd20482    1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568951067 140 LDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERL 180
Cdd:cd20482   81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARL 121
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
386-637 1.89e-29

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 117.81  E-value: 1.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 386 GEFTNLQGVSAASSGRIVVADSNNQCIQVFS-NEGQFKfrfgvrGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSP 464
Cdd:COG4257   14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFT------EYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 465 -EGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNksccvftfqpNGKLVGRF-GGRGATDRHF-----AGPHFVAVNNKNE 537
Cdd:COG4257   88 kTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQ----------GGNRIGRLdPATGEVTEFPlptggAGPYGIAVDPDGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 538 IVVTDFHNHSVKVYSADGEFLFKFgshgEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-SSGSFLSYINTSAEPLy 616
Cdd:COG4257  158 LWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEYPLPGGGAR- 232
                        250       260
                 ....*....|....*....|.
gi 568951067 617 gPQGLALTSDGHVVVADAGNH 637
Cdd:COG4257  233 -PYGVAVDGDGRVWFAESGAN 252
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
224-321 6.23e-25

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: 98.83  E-value: 6.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   224 AHETVATGEGLRQALVGQPASLTVTTKDKdgrlvrtGSAELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLS 303
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*...
gi 568951067   304 VLLYGQPVRGSPFRVRAL 321
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVG 91
Filamin pfam00630
Filamin/ABP280 repeat;
224-317 7.90e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 7.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  224 AHETVATGEGLRQALVGQPASLTVTTKDKDGrlvrtgsaELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLS 303
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGG--------EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 568951067  304 VLLYGQPVRGSPFR 317
Cdd:pfam00630  76 VKFNGQHIPGSPFK 89
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
23-55 1.01e-18

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: 80.05  E-value: 1.01e-18
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568951067  23 KTMEFYCEACETAMCGECRAGEHREHGTVLLRD 55
Cdd:cd19825   15 KTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
BBOX smart00336
B-Box-type zinc finger;
23-53 1.52e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.50  E-value: 1.52e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568951067    23 KTMEFYCEACETAMCGECRAGEHREHGTVLL 53
Cdd:smart00336  12 EPAEFFCEECGALLCRTCDEAEHRGHTVVLL 42
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
571-598 1.11e-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: 48.17  E-value: 1.11e-07
                          10        20
                  ....*....|....*....|....*...
gi 568951067  571 FNAPTGVAVDSNGNIIVADWGNSRIQVF 598
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
zf-B_box pfam00643
B-box zinc finger;
22-53 5.14e-07

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 46.31  E-value: 5.14e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568951067   22 MKTMEFYCEACETAMCGECRAGEHREHGTVLL 53
Cdd:pfam00643  11 EEPLTLYCNDCQELLCEECSVGEHRGHTVVPL 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
59-222 1.21e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  59 QHKAALQRQLEAVRGRLPQLSAAIALVggisQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKvLQT 138
Cdd:COG4717  132 QELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQ 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 139 QLDTLRQGQEHIGSSCSFAEQALRlgsAPEVLLVRKHMRERLAALAAQAFPerphENAQLELVLEVDGLRRSVLNLGALL 218
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELE---QLENELEAAALEERLKEARLLLLI----AAALLALLGLGGSLLSLILTIAGVL 279

                 ....
gi 568951067 219 TTSA 222
Cdd:COG4717  280 FLVL 283
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
399-645 2.13e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 51.01  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  399 SGRIVVADSNNQCIQVFSNEGQFKFRFGVRGR--------SPGQLQRPTGVAVDTNGDII-VADYDN---RWVSiFSPEg 466
Cdd:PLN02919  579 NNRLFISDSNHNRIVVTDLDGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKNLLyVADTENhalREID-FVNE- 656
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  467 KFKTKIGAGR---------------LMGPKGVAVDRNGHIIVV-----------DNKSCCVFTFQPNGKLVGRFGGRGaT 520
Cdd:PLN02919  657 TVRTLAGNGTkgsdyqggkkgtsqvLNSPWDVCFEPVNEKVYIamagqhqiweyNISDGVTRVFSGDGYERNLNGSSG-T 735
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  521 DRHFAGPHFVAVN-NKNEIVVTDFHNHSVKVYS---------ADG-----EFLFKFGSH-GEG-NGQFNAPTGVAVDSNG 583
Cdd:PLN02919  736 STSFAQPSGISLSpDLKELYIADSESSSIRALDlktggsrllAGGdptfsDNLFKFGDHdGVGsEVLLQHPLGVLCAKDG 815
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951067  584 NIIVADWGNSRIQVFDSSGSFLSYINTS-----------AEPLYGPQGLALTSDGHVVVADAGNHCFkayRYL 645
Cdd:PLN02919  816 QIYVADSYNHKIKKLDPATKRVTTLAGTgkagfkdgkalKAQLSEPAGLALGENGRLFVADTNNSLI---RYL 885
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
55-214 3.02e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    55 DVVEQHkAALQRQLEAVRGRLPQ----LSAAIALV---GGISQQLQERKAEALAQISAAFEDLEQALQQRKQA------L 121
Cdd:pfam01576  219 DLQEQI-AELQAQIAELRAQLAKkeeeLQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   122 VSDLESicgakqkvLQTQL-DTLrqgqehigsSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQL-E 199
Cdd:pfam01576  298 GEELEA--------LKTELeDTL---------DTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALeE 360
                          170
                   ....*....|....*
gi 568951067   200 LVLEVDGLRRSVLNL 214
Cdd:pfam01576  361 LTEQLEQAKRNKANL 375
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
44-163 4.28e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    44 EHREHGTVLLRD----VVEQHKAALQRQLEAVRGRLPQLSAAIAlvggisQQLQERKAEALAQISAAfedleQALQQRKQ 119
Cdd:TIGR00618  405 LQREQATIDTRTsafrDLQGQLAHAKKQQELQQRYAELCAAAIT------CTAQCEKLEKIHLQESA-----QSLKEREQ 473
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568951067   120 ALvSDLESICgakQKVLQTQLDTLRQGQEHIGSSCSFAEQALRL 163
Cdd:TIGR00618  474 QL-QTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
50-131 7.82e-03

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 39.06  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  50 TVLLRDV----VEQHKAALQRQLE--AVRGRLPQlSAAIALVGGIS--QQLQERKAEALAqISAAFEDLEQalqqrKQAL 121
Cdd:PRK08268  32 TVLLYDAragaAAAARDGIAARLAklVEKGKLTA-EQADAALARLRpvEALADLADCDLV-VEAIVERLDV-----KQAL 104
                         90
                 ....*....|
gi 568951067 122 VSDLESICGA 131
Cdd:PRK08268 105 FAQLEAIVSP 114
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
373-646 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: 584.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 373 ELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVA 452
Cdd:cd14960    1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 453 DYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAV 532
Cdd:cd14960   81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 533 NNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 612
Cdd:cd14960  161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568951067 613 EPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ 646
Cdd:cd14960  241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
382-642 1.14e-98

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: 302.70  E-value: 1.14e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 382 GREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSI 461
Cdd:cd05819    1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFNEPAGVAVDSDGNLYVADTGNHRIQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 462 FSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKN 536
Cdd:cd05819   81 FDPDGNFLASFGgsgdgDGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGSGGSGPGQFNGPTGVAVDSDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 537 EIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFL----SYINTSA 612
Cdd:cd05819  161 NIYVADTGNHRIQVFDPDGNFLTTFGSTGTGPGQFNYPTGIAVDSDGNIYVADSGNNRVQVFDPDGAGFggngNFLGSDG 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 568951067 613 EpLYGPQGLALTSDGHVVVADAGNHCFKAY 642
Cdd:cd05819  241 Q-FNRPSGLAVDSDGNLYVADTGNNRIQVF 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
374-638 1.25e-96

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: 298.31  E-value: 1.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 374 LVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVAD 453
Cdd:cd14954    9 PLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRDGQFDRPAGVAVNSRGRIIVAD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 454 YDNRWVSIFSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPH 528
Cdd:cd14954   89 KDNHRIQVFDLNGRFLLKFGergtkNGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPGQLDSPR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 529 FVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI 608
Cdd:cd14954  169 GVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSF 248
                        250       260       270
                 ....*....|....*....|....*....|...
gi 568951067 609 NTSAEP---LYGPQGLALTSDGHVVVADAGNHC 638
Cdd:cd14954  249 GTEGNGegqFDRPSGVAVTPDGRIVVVDRGNHR 281
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
379-638 4.96e-82

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: 260.20  E-value: 4.96e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 379 GSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRW 458
Cdd:cd14955    6 GSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVADTGNHR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 459 VSIFSPEGKFKTK-----IGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVN 533
Cdd:cd14955   86 IQKFDSTGTFLTKwgssgSGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQFNSPTGIAVD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 534 NKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLS---YINT 610
Cdd:cd14955  166 SAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVDSAGNVYVADTGNNRIQKFDSSGTFITkwgSEGS 245
                        250       260
                 ....*....|....*....|....*...
gi 568951067 611 SAEPLYGPQGLALTSDGHVVVADAGNHC 638
Cdd:cd14955  246 GDGQFNSPSGIAVDSAGNVYVADSGNNR 273
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
376-637 1.33e-78

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: 251.03  E-value: 1.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 376 FRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYD 455
Cdd:cd14957    5 YAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYSYSIGSGGTGSGQFNSPYGIAVDSNGNIYVADTD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 456 NRWVSIFSPEGKFKTKIGA-----GRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFV 530
Cdd:cd14957   85 NNRIQVFNSSGVYQYSIGTggsgdGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTSSGTFSYSIGSGGTGPGQFNGPQGI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 531 AVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINT 610
Cdd:cd14957  165 AVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSGAYQYSIGT 244
                        250       260       270
                 ....*....|....*....|....*....|
gi 568951067 611 SAEPLYG---PQGLALTSDGHVVVADAGNH 637
Cdd:cd14957  245 SGSGNGQfnyPYGIAVDNDGKIYVADSNNN 274
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
379-637 4.51e-70

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: 228.71  E-value: 4.51e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 379 GSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRW 458
Cdd:cd14956    3 GGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 459 VSIFSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVN 533
Cdd:cd14956   83 IQVFTLTGELQTIGGssgsgPGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIEPGSFNYPRGVAVD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 534 NKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI---NT 610
Cdd:cd14956  163 PDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWgspGT 242
                        250       260
                 ....*....|....*....|....*..
gi 568951067 611 SAEPLYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14956  243 GPGQFKNPWGVVVDADGTVYVADSNNN 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
414-637 1.11e-65

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: 217.42  E-value: 1.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 414 VFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGA-----GRLMGPKGVAVDRN 488
Cdd:cd14954    2 DYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSygsrdGQFDRPAGVAVNSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 489 GHIIVVD--NKSCCVFTfqPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGE 566
Cdd:cd14954   82 GRIIVADkdNHRIQVFD--LNGRFLLKFGERGTKNGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568951067 567 GNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAE---PLYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14954  160 GPGQLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSgngQFKRPRGVAVDDEGNIIVADSGNH 233
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
378-599 1.20e-64

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: 214.44  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 378 VGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNR 457
Cdd:cd14957   54 IGSGGTGSGQFNSPYGIAVDSNGNIYVADTDNNRIQVFNSSGVYQYSIGTGGSGDGQFNGPYGIAVDSNGNIYVADTGNH 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 458 WVSIFSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAV 532
Cdd:cd14957  134 RIQVFTSSGTFSYSIGsggtgPGQFNGPQGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGPGQFSDPYGIAV 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568951067 533 NNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 599
Cdd:cd14957  214 DSDGNIYVADTGNHRIQVFTSSGAYQYSIGTSGSGNGQFNYPYGIAVDNDGKIYVADSNNNRIQVFN 280
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
379-643 8.14e-63

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: 209.44  E-value: 8.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 379 GSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRW 458
Cdd:cd14961    1 GSFGGWPGTLNNPTGVAVTPTGRVVVADDGNKRIQVFDSDGNCLQQFGPKGDAGQDIRYPLDVAVTPDGHIVVTDAGDRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 459 VSIFSPEGKFKTKIGaGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLvGRFGGRGATDRHFAGPHFVAVNNKNEI 538
Cdd:cd14961   81 VKVFSFDGRLKLFVR-KSFSLPWGVAVNPSGEILVTDSEAGKLFVLTVDFKL-GILKKGQKLCSQLCRPRFVAVSRLGAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 539 VVTD--------FHNHSVKVYSADGEFLFKFGS--HGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI 608
Cdd:cd14961  159 AVTEhlfangtrSSSTRVKVFSSGGQLLGQIDSfgLNLVFPSLICASGVAFDSEGNVIVADTGSGAILCLGKPEGFPILK 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 568951067 609 NTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYR 643
Cdd:cd14961  239 PIVTQGLSRPVGLAVTPDGSLVVLDSGNHCVKIYK 273
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
421-637 2.25e-61

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: 205.58  E-value: 2.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 421 FKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGrLMG------PKGVAVDRNGHIIVV 494
Cdd:cd14957    3 FSYAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYSYSIGSG-GTGsgqfnsPYGIAVDSNGNIYVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 495 DNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAP 574
Cdd:cd14957   82 DTDNNRIQVFNSSGVYQYSIGTGGSGDGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTSSGTFSYSIGSGGTGPGQFNGP 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951067 575 TGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEP---LYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14957  162 QGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGpgqFSDPYGIAVDSDGNIYVADTGNH 227
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
425-637 3.52e-60

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: 202.42  E-value: 3.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 425 FGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSC 499
Cdd:cd14955    5 WGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGssgsgDGQFYSPTGIAVDSDGNVYVADTGNH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 500 CVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAV 579
Cdd:cd14955   85 RIQKFDSTGTFLTKWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQFNSPTGIAV 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951067 580 DSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEP---LYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14955  165 DSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGdgqFNAPYGIAVDSAGNVYVADTGNN 225
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
396-636 2.33e-59

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: 199.82  E-value: 2.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 396 AASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAG 475
Cdd:cd14963   16 AVSDGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKYFPEK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 476 R----LMGPKGVAVDRnGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVY 551
Cdd:cd14963   96 KdrvkLISPAGLAIDD-GKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 552 SADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA---EPLYGPQGLALTSDGH 628
Cdd:cd14963  175 DKNGKFIKELNGSPDGKSGFVNPRGIAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGkddGQFNLPNGLFIDDDGR 254

                 ....*...
gi 568951067 629 VVVADAGN 636
Cdd:cd14963  255 LYVTDREN 262
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
377-598 5.08e-56

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: 191.34  E-value: 5.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 377 RVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDN 456
Cdd:cd14956   48 RFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDRIQVFTLTGELQTIGGSSGSGPGQFNAPRGVAVDADGNLYVADFGN 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 457 RWVSIFSPEGKF-----KTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVA 531
Cdd:cd14956  128 QRIQKFDPDGSFlrqwgGTGIEPGSFNYPRGVAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQFNYPYGIA 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568951067 532 VNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 598
Cdd:cd14956  208 IDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGTVYVADSNNNRVQRF 274
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
373-645 8.79e-55

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: 187.86  E-value: 8.79e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 373 ELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAV-DTNGDIIV 451
Cdd:cd14959    6 IIHCKFGESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQVFDKEGEFKFQFGIPGKRDGQLWYPNKVAVcRVTGRYVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 452 ADYDN--RWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGgrgaTDRHFAGPHF 529
Cdd:cd14959   86 TDRGNprHRMQIFTKRGQFVRKFGARYLQHVRGLTVDAAGHIIVVESKVMRVFIFDESGNVLKWFD----CSKYLEEPSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 530 VAVNNkNEIVVTDFHNHSVKVYSADGEFLFKFGshgeGNGQFNAPTGVAVDSNGNIIVADWGNSR--IQVFDSSGSFLSY 607
Cdd:cd14959  162 VAVND-NEIYICDNKGHCVVVFNYDGQFLRRIG----GEGITNYPIGVDISSAGDVLVADNHGNHfhVTVFTRDGQLISE 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568951067 608 INTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYL 645
Cdd:cd14959  237 FECPRVKHSRCCGLALTSEGSIVTLSKHNHHVLVFNTL 274
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
383-645 7.80e-52

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: 180.09  E-value: 7.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 383 REKGEFTNLQGVSAASSGRIVVADSNNQCIQVFsNEGQFKFRFgVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIF 462
Cdd:cd14962    6 RPKEALTRPYGVAADGRGRIYVADTGRGAVFVF-DLPNGKVFV-IGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 463 SPEGKFKTKIGAGRLMG-PKGVAVD-RNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVV 540
Cdd:cd14962   84 DRDGKFLRAIGAGALFKrPTGIAVDpAGKRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNLPTDLAVDRDGNLYV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 541 TDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI-NTSAEP--LYG 617
Cdd:cd14962  164 TDTMNFRVQIFDADGKFLRSFGERGDGPGSFARPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVgGPGSGPgeFYL 243
                        250       260
                 ....*....|....*....|....*...
gi 568951067 618 PQGLALTSDGHVVVADAGNHCFKAYRYL 645
Cdd:cd14962  244 PSGIAIDKDDRIYVVDQFNRRIQVFQYL 271
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
425-637 2.73e-46

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: 165.15  E-value: 2.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 425 FGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTkigagrlmgpkgvavdrnghiivvdnksccvftf 504
Cdd:cd14956    2 WGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLR---------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 505 qpngklvgRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGN 584
Cdd:cd14956   48 --------RFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDRIQVFTLTGELQTIGGSSGSGPGQFNAPRGVAVDADGN 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568951067 585 IIVADWGNSRIQVFDSSGSFL-SYINTSAEP--LYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14956  120 LYVADFGNQRIQKFDPDGSFLrQWGGTGIEPgsFNYPRGVAVDPDGTLYVADTYND 175
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
375-598 1.50e-40

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: 148.89  E-value: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 375 VFRVGSRGREKgeFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGvrgrSPGQLQRPTGVAVD-TNGDIIVAD 453
Cdd:cd14962   45 VFVIGNAGPNR--FVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRAIG----AGALFKRPTGIAVDpAGKRLYVVD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 454 YDNRWVSIFSPEGKFKTKIG-----AGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPH 528
Cdd:cd14962  119 TLAHKVKVFDLDGRLLFDIGkrgsgPGEFNLPTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGERGDGPGSFARPK 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 529 FVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 598
Cdd:cd14962  199 GIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRRIQVF 268
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
60-186 1.46e-38

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 138.55  E-value: 1.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    60 HKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQ 139
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568951067   140 LDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQ 186
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
432-636 1.64e-38

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: 144.33  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 432 PGQLQRPTGVAVDTNGD-IIVADYDNRWVS--------------------IFSPEGKFKTKIGAGRLMGPKGVAVDRNGH 490
Cdd:cd14958    9 SLKLGQVSGVAVDSLGNgVVFHRGGRVWDAnsfdanvyvfkgpieedtilVFDPDGGFLRSWGAGLFYMPHGLTIDPDGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 491 IIVVDNKSCCVFTFQPNGKLV-----GRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFH-NHSVKVYSADGEFLFKFGSH 564
Cdd:cd14958   89 IWVTDVGLHQVFKFDPEGKLLplltlGERGEPGSDQTHFCKPTDVAVAPDGDIFVADGYcNSRIVKFSPDGKLLKSWGEP 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951067 565 GEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLS-YINTSAEPLYgpqGLALTSDGHVVVADAGN 636
Cdd:cd14958  169 GSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLTeWTNPELGRPY---ALAIDPDGLLYVVDGPP 238
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
388-637 1.43e-37

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: 142.28  E-value: 1.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 388 FTNLQGVSAASSGRIVVADSNNQCI---------QVFSNEGQFKFRFGvrGRSPGQLQRPTGVAVDTNGDIIVADYDNRW 458
Cdd:cd14953   22 FNSPSGVAVDAAGNLYVADRGNHRIrkitpdgvvTTVAGTGTAGFADG--GGAAAQFNTPSGVAVDAAGNLYVADTGNHR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 459 VSIFSPEGKFKTKIGAG-------------RLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLV--------GRFGGR 517
Cdd:cd14953  100 IRKITPDGVVSTLAGTGtagfsddggataaQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVTtvagtggaGYAGDG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 518 GATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEG--------NGQFNAPTGVAVDSNGNIIVAD 589
Cdd:cd14953  180 PATAAQFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGTAGfsgdggatAAQLNNPTGVAVDAAGNLYVAD 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568951067 590 WGNSRIQVFDSSG----------SFLSYINTSAE-PLYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14953  260 SGNHRIRKITPAGvvttvagggaGFSGDGGPATSaQFNNPTGVAVDAAGNLYVADTGNN 318
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
60-180 2.25e-37

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: 134.97  E-value: 2.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  60 HKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQ 139
Cdd:cd20482    1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568951067 140 LDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERL 180
Cdd:cd20482   81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARL 121
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
514-638 5.69e-36

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: 136.55  E-value: 5.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 514 FGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNS 593
Cdd:cd14955    5 WGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVADTGNH 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568951067 594 RIQVFDSSGSFLSYINTS---AEPLYGPQGLALTSDGHVVVADAGNHC 638
Cdd:cd14955   85 RIQKFDSTGTFLTKWGSSgsgDGQFNSPSGIAVDSAGNVYVTDSGNNR 132
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
434-638 2.19e-34

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: 133.42  E-value: 2.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 434 QLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAG------------RLMGPKGVAVDRNGHIIVVDNKSCC- 500
Cdd:cd14953   21 RFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGtagfadgggaaaQFNTPSGVAVDAAGNLYVADTGNHRi 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 501 --------VFTFQPNGKlVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEF-----LFKFGSHGEG 567
Cdd:cd14953  101 rkitpdgvVSTLAGTGT-AGFSDDGGATAAQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVttvagTGGAGYAGDG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 568 NG---QFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSF------------LSYINTSAEpLYGPQGLALTSDGHVVVA 632
Cdd:cd14953  180 PAtaaQFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVttvagtgtagfsGDGGATAAQ-LNNPTGVAVDAAGNLYVA 258

                 ....*.
gi 568951067 633 DAGNHC 638
Cdd:cd14953  259 DSGNHR 264
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
518-637 4.64e-30

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: 119.32  E-value: 4.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 518 GATDRHFAGPHFVAVNNKNeIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQV 597
Cdd:cd14963    3 GPFGDPLNKPMGVAVSDGR-IYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQV 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568951067 598 FDSSGSFLSYI--NTSAEPLYGPQGLALtSDGHVVVADAGNH 637
Cdd:cd14963   82 FDPDGKFLKYFpeKKDRVKLISPAGLAI-DDGKLYVSDVKKH 122
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
386-637 1.89e-29

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 117.81  E-value: 1.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 386 GEFTNLQGVSAASSGRIVVADSNNQCIQVFS-NEGQFKfrfgvrGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSP 464
Cdd:COG4257   14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFT------EYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 465 -EGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNksccvftfqpNGKLVGRF-GGRGATDRHF-----AGPHFVAVNNKNE 537
Cdd:COG4257   88 kTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQ----------GGNRIGRLdPATGEVTEFPlptggAGPYGIAVDPDGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 538 IVVTDFHNHSVKVYSADGEFLFKFgshgEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-SSGSFLSYINTSAEPLy 616
Cdd:COG4257  158 LWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEYPLPGGGAR- 232
                        250       260
                 ....*....|....*....|.
gi 568951067 617 gPQGLALTSDGHVVVADAGNH 637
Cdd:COG4257  233 -PYGVAVDGDGRVWFAESGAN 252
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
374-495 8.60e-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: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 113.07  E-value: 8.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 374 LVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVAD 453
Cdd:cd14962  133 LLFDIGKRGSGPGEFNLPTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGERGDGPGSFARPKGIAVDSEGNIYVVD 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568951067 454 --YDNrwVSIFSPEGKF-----KTKIGAGRLMGPKGVAVDRNGHIIVVD 495
Cdd:cd14962  213 aaFDN--VQIFNPEGELlltvgGPGSGPGEFYLPSGIAIDKDDRIYVVD 259
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
370-598 2.30e-26

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: 108.92  E-value: 2.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 370 IEDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFgvrgrspgqlqrptgvavdtNGDi 449
Cdd:cd14963  129 LEGKLLLEFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKEL--------------------NGS- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 450 ivadydnrwvsifspegkfktKIGAGRLMGPKGVAVDRNGHIIVVDNKSccvftfqpngklvgrfggrgatdrhfagphf 529
Cdd:cd14963  188 ---------------------PDGKSGFVNPRGIAVDPDGNLYVVDNLS------------------------------- 215
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951067 530 vavnnkneivvtdfhnHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 598
Cdd:cd14963  216 ----------------HRVYVFDEQGKELFTFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
392-595 3.69e-26

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: 109.54  E-value: 3.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 392 QGVSAASSGRIVVADSNNQCIQVFSNEGQF---------KFRFGVrGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIF 462
Cdd:cd14953   80 SGVAVDAAGNLYVADTGNHRIRKITPDGVVstlagtgtaGFSDDG-GATAAQFNYPTGVAVDAAGNLYVADTGNHRIRKI 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 463 SPEGKFKTKIGAG-------------RLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKL--------VGRFGGRGATD 521
Cdd:cd14953  159 TPDGVVTTVAGTGgagyagdgpataaQFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVttvagtgtAGFSGDGGATA 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 522 RHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGE----FLFKFGSHGEGNG----QFNAPTGVAVDSNGNIIVADWGNS 593
Cdd:cd14953  239 AQLNNPTGVAVDAAGNLYVADSGNHRIRKITPAGVvttvAGGGAGFSGDGGPatsaQFNNPTGVAVDAAGNLYVADTGNN 318

                 ..
gi 568951067 594 RI 595
Cdd:cd14953  319 RI 320
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
432-637 8.46e-26

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 107.41  E-value: 8.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 432 PGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLV 511
Cdd:COG4257   13 PAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGEI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 512 GRFggrgATDRHFAGPHFVAVNNKNEIVVTDFHNHSV-KVYSADGEFLFKFGSHGEGNgqfnaPTGVAVDSNGNIIVADW 590
Cdd:COG4257   93 TTF----ALPGGGSNPHGIAFDPDGNLWFTDQGGNRIgRLDPATGEVTEFPLPTGGAG-----PYGIAVDPDGNLWVTDF 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568951067 591 GNSRIQVFDSSGSFLSYINTSAePLYGPQGLALTSDGHVVVADAGNH 637
Cdd:COG4257  164 GANAIGRIDPDTGTLTEYALPT-PGAGPRGLAVDPDGNLWVADTGSG 209
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
224-321 6.23e-25

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: 98.83  E-value: 6.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   224 AHETVATGEGLRQALVGQPASLTVTTKDKdgrlvrtGSAELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLS 303
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*...
gi 568951067   304 VLLYGQPVRGSPFRVRAL 321
Cdd:smart00557  74 VKFGGEHIPGSPFTVKVG 91
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
388-637 3.55e-24

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: 101.90  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 388 FTNL---QGVSAASSGRIVVADS-NNQCIQVFSN-EGQFKFRFGvrgrspgQLQRPTGVAVDTNGDIIVADYDNRWVSIF 462
Cdd:cd14952    6 FTGLdgpGGVAVDAAGNVYVADSgNNRVLKLAAGsTTQTVLPFT-------GLYQPQGVAVDAAGTVYVTDFGNNRVLKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 463 SPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNksccvftfqPNGKLVGRFGGRGA-TDRHFAG---PHFVAVNNKNEI 538
Cdd:cd14952   79 AAGSTTQTVLPFTGLNDPTGVAVDAAGNVYVADT---------GNNRVLKLAAGSNTqTVLPFTGlsnPDGVAVDGAGNV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 539 VVTDFHNHSVKVYSAdgeflfkfGSHGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRIQVFDSsGSflsyiNTSAE-P 614
Cdd:cd14952  150 YVTDTGNNRVLKLAA--------GSTTQTVLPFtglNSPSGVAVDTAGNVYVTDHGNNRVLKLAA-GS-----TTPTVlP 215
                        250       260
                 ....*....|....*....|....*.
gi 568951067 615 ---LYGPQGLALTSDGHVVVADAGNH 637
Cdd:cd14952  216 ftgLNGPLGVAVDAAGNVYVADRGND 241
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
557-637 3.70e-24

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: 102.65  E-value: 3.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 557 FLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTS-AEP--LYGPQGLALTSDGHVVVAD 633
Cdd:cd14955    1 FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSgSGDgqFYSPTGIAVDSDGNVYVAD 80

                 ....
gi 568951067 634 AGNH 637
Cdd:cd14955   81 TGNH 84
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
384-607 1.87e-23

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 100.48  E-value: 1.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 384 EKGEFTNLQGVSAASSGRIVVADSNNQCIQVFS-NEGQFKfRFGVrgrsPGQLQRPTGVAVDTNGDIIVADYDNRWVSIF 462
Cdd:COG4257   54 PLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDpKTGEIT-TFAL----PGGGSNPHGIAFDPDGNLWFTDQGGNRIGRL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 463 SPE-GKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFggrgATDRHFAGPHFVAVNNKNEIVVT 541
Cdd:COG4257  129 DPAtGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVA 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951067 542 DFHNHSVKVYSADGEFLFKFGSHGEGNGqfnaPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSY 607
Cdd:COG4257  205 DTGSGRIGRFDPKTGTVTEYPLPGGGAR----PYGVAVDGDGRVWFAESGANRIVRFDPDTELTEY 266
Filamin pfam00630
Filamin/ABP280 repeat;
224-317 7.90e-23

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 92.74  E-value: 7.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  224 AHETVATGEGLRQALVGQPASLTVTTKDKDGrlvrtgsaELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLS 303
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGG--------EGEVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 568951067  304 VLLYGQPVRGSPFR 317
Cdd:pfam00630  76 VKFNGQHIPGSPFK 89
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
412-599 1.51e-22

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: 98.49  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 412 IQVFSNEGQFKFRFGvrgrsPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMG----------PK 481
Cdd:cd14958   57 ILVFDPDGGFLRSWG-----AGLFYMPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEpgsdqthfckPT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 482 GVAVDRNGHIIVVD---NKscCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFL 558
Cdd:cd14958  132 DVAVAPDGDIFVADgycNS--RIVKFSPDGKLLKSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFL 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 559 --------------------------------------------------FKFGSHGEGNGQFNAPTGVAVDSNGNIIVA 588
Cdd:cd14958  210 tewtnpelgrpyalaidpdgllyvvdgpprlnrslpvrgfvirigkglilGRFGPGGKAPGQFQNPHDIAVDSGGDIYVG 289
                        250
                 ....*....|.
gi 568951067 589 DWGNSRIQVFD 599
Cdd:cd14958  290 ELGPNRVQKFV 300
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
549-637 5.00e-21

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: 93.77  E-value: 5.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 549 KVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFL----SYINTSAEpLYGPQGLALT 624
Cdd:cd14954    1 RDYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLrkfgSYGSRDGQ-FDRPAGVAVN 79
                         90
                 ....*....|...
gi 568951067 625 SDGHVVVADAGNH 637
Cdd:cd14954   80 SRGRIIVADKDNH 92
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
514-638 1.01e-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: 90.67  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 514 FGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGE--FLFKFGSHGEGNG-----QFNAPTGVAVDSNGNII 586
Cdd:cd14953   12 FSGGGGTAARFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVvtTVAGTGTAGFADGggaaaQFNTPSGVAVDAAGNLY 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951067 587 VADWGNSRIQVFDSSG-----------SFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHC 638
Cdd:cd14953   92 VADTGNHRIRKITPDGvvstlagtgtaGFSDDGGATAAQFNYPTGVAVDAAGNLYVADTGNHR 154
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
23-55 1.01e-18

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: 80.05  E-value: 1.01e-18
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568951067  23 KTMEFYCEACETAMCGECRAGEHREHGTVLLRD 55
Cdd:cd19825   15 KTMEFYCESCETAMCRECTEGEHREHVTVPLRD 47
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
560-642 2.63e-18

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 85.41  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 560 KFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINT---SAEPLYGPQGLALTSDGHVVVADAGN 636
Cdd:cd14956    1 SWGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTtgdGPGQFGRPRGLAVDKDGWLYVADYWG 80

                 ....*.
gi 568951067 637 HCFKAY 642
Cdd:cd14956   81 DRIQVF 86
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
374-462 3.59e-18

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 85.03  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 374 LVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVAD 453
Cdd:cd14956  186 FLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGTVYVAD 265

                 ....*....
gi 568951067 454 YDNRWVSIF 462
Cdd:cd14956  266 SNNNRVQRF 274
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
373-463 4.70e-18

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: 84.62  E-value: 4.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 373 ELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVA 452
Cdd:cd14957  190 TFQYTFGSSGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSGAYQYSIGTSGSGNGQFNYPYGIAVDNDGKIYVA 269
                         90
                 ....*....|.
gi 568951067 453 DYDNRWVSIFS 463
Cdd:cd14957  270 DSNNNRIQVFN 280
Bbox2_TRIM2-like cd19759
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and ...
23-55 1.12e-16

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: 74.02  E-value: 1.12e-16
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568951067  23 KTMEFYCEACETAMCGECRAGEHREHGTVLLRD 55
Cdd:cd19759   10 ETLEFYCESCETAVCRECTAGEHNEHRTVLLKD 42
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
379-464 3.17e-14

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: 73.39  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 379 GSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRW 458
Cdd:cd14962  185 GERGDGPGSFARPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRR 264

                 ....*.
gi 568951067 459 VSIFSP 464
Cdd:cd14962  265 IQVFQY 270
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
439-638 9.54e-13

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 68.18  E-value: 9.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 439 TGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGH-IIVVDNKSCCVFTFQP-NGKLVGRFgg 516
Cdd:COG3391   29 GLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRrLYVANSGSGRVSVIDLaTGKVVATI-- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 517 rgatdRHFAGPHFVAVN-NKNEIVVTDFHNHSVKVYS-ADGEFLFKFGShgeGNGqfnaPTGVAVDSNGN-IIVADWGNS 593
Cdd:COG3391  107 -----PVGGGPRGLAVDpDGGRLYVADSGNGRVSVIDtATGKVVATIPV---GAG----PHGIAVDPDGKrLYVANSGSN 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568951067 594 RI----QVFD-SSGSFLSYINTSAeplyGPQGLALTSDG-HVVVADAGNHC 638
Cdd:COG3391  175 TVsvivSVIDtATGKVVATIPVGG----GPVGVAVSPDGrRLYVANRGSNT 221
Bbox2_TRIM2_C-VII cd19824
B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar ...
25-55 1.40e-12

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: 62.38  E-value: 1.40e-12
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568951067  25 MEFYCEACETAMCGECRAGEHREHGTVLLRD 55
Cdd:cd19824   12 MEFYCQSCETAMCQECTEGEHAEHPTVPLKD 42
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
561-638 2.38e-12

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: 68.33  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 561 FGSHGEG--NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINT----------SAEPLYGPQGLALTSDGH 628
Cdd:cd14953   10 AGFSGGGgtAARFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTgtagfadgggAAAQFNTPSGVAVDAAGN 89
                         90
                 ....*....|
gi 568951067 629 VVVADAGNHC 638
Cdd:cd14953   90 LYVADTGNHR 99
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
374-599 3.76e-12

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 66.64  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 374 LVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVAD 453
Cdd:COG3391    7 LLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVAN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 454 YDNRWVSIFSPE-GKFKTKIGAGRlmGPKGVAVDRNG-HIIVVDNKSCCVFTF-QPNGKLVGRFGGrgatdrhFAGPHFV 530
Cdd:COG3391   87 SGSGRVSVIDLAtGKVVATIPVGG--GPRGLAVDPDGgRLYVADSGNGRVSVIdTATGKVVATIPV-------GAGPHGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 531 AVN-NKNEIVVTDFHNHSVKVY-----SADGEFL--FKFGSHgegngqfnaPTGVAVDSNGNIIV--------ADWGNSR 594
Cdd:COG3391  158 AVDpDGKRLYVANSGSNTVSVIvsvidTATGKVVatIPVGGG---------PVGVAVSPDGRRLYvanrgsntSNGGSNT 228

                 ....*
gi 568951067 595 IQVFD 599
Cdd:COG3391  229 VSVID 233
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
437-605 7.89e-12

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: 66.07  E-value: 7.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 437 RPTGVAVDTNGDIIVADYDNRwVSIFSPE-GKFKTKIGAG--RLMGPKGVAVDRNGHIivvdnksccVFT----FQPNGK 509
Cdd:COG3386   50 RPNGLAFDPDGRLLVADHGRG-LVRFDPAdGEVTVLADEYgkPLNRPNDGVVDPDGRL---------YFTdmgeYLPTGA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 510 LVgRFGGRGATDRHFAGPHF---VAVNNKNEIV-VTDFHNHSVKVY--SADGEFLFK--FGSHGEGNGqfnAPTGVAVDS 581
Cdd:COG3386  120 LY-RVDPDGSLRVLADGLTFpngIAFSPDGRTLyVADTGAGRIYRFdlDADGTLGNRrvFADLPDGPG---GPDGLAVDA 195
                        170       180
                 ....*....|....*....|....
gi 568951067 582 NGNIIVADWGNSRIQVFDSSGSFL 605
Cdd:COG3386  196 DGNLWVALWGGGGVVRFDPDGELL 219
BBOX smart00336
B-Box-type zinc finger;
23-53 1.52e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.50  E-value: 1.52e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568951067    23 KTMEFYCEACETAMCGECRAGEHREHGTVLL 53
Cdd:smart00336  12 EPAEFFCEECGALLCRTCDEAEHRGHTVVLL 42
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
571-598 1.11e-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: 48.17  E-value: 1.11e-07
                          10        20
                  ....*....|....*....|....*...
gi 568951067  571 FNAPTGVAVDSNGNIIVADWGNSRIQVF 598
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
471-644 2.09e-07

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: 52.59  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 471 KIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFggrgATDRHFAGphFVAVNNKNEIVVTDfHNHSVKV 550
Cdd:COG3386    1 KLADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVF----AEPSGRPN--GLAFDPDGRLLVAD-HGRGLVR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 551 YS-ADGEFLFKFGSHGEGNGQFNaptGVAVDSNGNIIVAD----WGNSRIQVFDSSGSflsyINTSAEPLYGPQGLALTS 625
Cdd:COG3386   74 FDpADGEVTVLADEYGKPLNRPN---DGVVDPDGRLYFTDmgeyLPTGALYRVDPDGS----LRVLADGLTFPNGIAFSP 146
                        170       180
                 ....*....|....*....|
gi 568951067 626 DG-HVVVADAGNHCFKAYRY 644
Cdd:COG3386  147 DGrTLYVADTGAGRIYRFDL 166
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
426-637 4.78e-07

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: 52.19  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 426 GVRGRSPG-----QLQRPTGVAVDTNGDIIVADYDN-RWVSIFSPEGKFKT----------KIGAGR-----LMGPKGVA 484
Cdd:cd14951    4 GERGLKDGsfaeaSFNEPQGLALLPGNILYVADTENhALRKIDLETGTVTTlagtgeqgrdGEGGGPgreqpLSSPWDVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 485 VDRNGHIIVVdnksCC-----VFTFQPNGKLVGRFGGRG---------ATDRHFAGPHFVAVNNKNEIVV---------- 540
Cdd:cd14951   84 WGPEDDILYI----AMagthqIWAYDLDTGTCRVFAGSGnegnrngpyPHEAWFAQPSGLSLAGWGELFVadsessaira 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 541 ---TDFHNHSVKVYSADGEFLFKFGsHGEGNGqFNA----PTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAE 613
Cdd:cd14951  160 vslKDGGVKTLVGGTRVGTGLFDFG-DRDGPG-AEAllqhPLGVAALPDGSVYVADTYNHKIKRVDPATGEVSTLAGTGK 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568951067 614 PLYG--------PQGLALTSDGHVVVADAGNH 637
Cdd:cd14951  238 AGYKdleaqfsePSGLVVDGDGRLYVADTNNH 269
zf-B_box pfam00643
B-box zinc finger;
22-53 5.14e-07

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 46.31  E-value: 5.14e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568951067   22 MKTMEFYCEACETAMCGECRAGEHREHGTVLL 53
Cdd:pfam00643  11 EEPLTLYCNDCQELLCEECSVGEHRGHTVVPL 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
59-222 1.21e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  59 QHKAALQRQLEAVRGRLPQLSAAIALVggisQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKvLQT 138
Cdd:COG4717  132 QELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQ 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 139 QLDTLRQGQEHIGSSCSFAEQALRlgsAPEVLLVRKHMRERLAALAAQAFPerphENAQLELVLEVDGLRRSVLNLGALL 218
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELE---QLENELEAAALEERLKEARLLLLI----AAALLALLGLGGSLLSLILTIAGVL 279

                 ....
gi 568951067 219 TTSA 222
Cdd:COG4717  280 FLVL 283
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
431-638 1.46e-06

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: 50.28  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 431 SPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRlMGPKGVAVDRNGHIIVVDNKSCcVFTFQP-NGK 509
Cdd:COG3386    3 ADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPS-GRPNGLAFDPDGRLLVADHGRG-LVRFDPaDGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 510 ---LVGRFGGRgatdrhFAGPHFVAVNNKNEIVVTDFHNH----SVKVYSADGEF--LFkfgshgegnGQFNAPTGVAVD 580
Cdd:COG3386   81 vtvLADEYGKP------LNRPNDGVVDPDGRLYFTDMGEYlptgALYRVDPDGSLrvLA---------DGLTFPNGIAFS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951067 581 SNGNI-IVADWGNSRIQVFD--SSGSfLS----YINTSAEPlYGPQGLALTSDGHVVVADAGNHC 638
Cdd:COG3386  146 PDGRTlYVADTGAGRIYRFDldADGT-LGnrrvFADLPDGP-GGPDGLAVDADGNLWVALWGGGG 208
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
25-61 2.11e-06

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: 44.99  E-value: 2.11e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568951067  25 MEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHK 61
Cdd:cd19796   12 LRLYCDTCSVPICRECTMGEHRGHSFIYLQEAVQDSK 48
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
399-645 2.13e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 51.01  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  399 SGRIVVADSNNQCIQVFSNEGQFKFRFGVRGR--------SPGQLQRPTGVAVDTNGDII-VADYDN---RWVSiFSPEg 466
Cdd:PLN02919  579 NNRLFISDSNHNRIVVTDLDGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKNLLyVADTENhalREID-FVNE- 656
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  467 KFKTKIGAGR---------------LMGPKGVAVDRNGHIIVV-----------DNKSCCVFTFQPNGKLVGRFGGRGaT 520
Cdd:PLN02919  657 TVRTLAGNGTkgsdyqggkkgtsqvLNSPWDVCFEPVNEKVYIamagqhqiweyNISDGVTRVFSGDGYERNLNGSSG-T 735
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  521 DRHFAGPHFVAVN-NKNEIVVTDFHNHSVKVYS---------ADG-----EFLFKFGSH-GEG-NGQFNAPTGVAVDSNG 583
Cdd:PLN02919  736 STSFAQPSGISLSpDLKELYIADSESSSIRALDlktggsrllAGGdptfsDNLFKFGDHdGVGsEVLLQHPLGVLCAKDG 815
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951067  584 NIIVADWGNSRIQVFDSSGSFLSYINTS-----------AEPLYGPQGLALTSDGHVVVADAGNHCFkayRYL 645
Cdd:PLN02919  816 QIYVADSYNHKIKKLDPATKRVTTLAGTgkagfkdgkalKAQLSEPAGLALGENGRLFVADTNNSLI---RYL 885
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
524-551 3.04e-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: 43.93  E-value: 3.04e-06
                          10        20
                  ....*....|....*....|....*...
gi 568951067  524 FAGPHFVAVNNKNEIVVTDFHNHSVKVY 551
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
480-599 3.05e-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: 49.50  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 480 PKGVAVDRNGHIIVVD-------------NKSCCVFTFQPNGKLVGRFG---GRGATDR--HfagPHFVAVNNKNEIVVT 541
Cdd:cd14951  136 PSGLSLAGWGELFVADsessairavslkdGGVKTLVGGTRVGTGLFDFGdrdGPGAEALlqH---PLGVAALPDGSVYVA 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951067 542 DFHNHSVKVY-SADGE--FLFKFGSHGEGN--GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 599
Cdd:cd14951  213 DTYNHKIKRVdPATGEvsTLAGTGKAGYKDleAQFSEPSGLVVDGDGRLYVADTNNHRIRRLD 275
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
571-638 4.00e-06

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 48.86  E-value: 4.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951067 571 FNAPTGVAVDSNGNIIVADWGNSRIQVFD-SSGSFLSYintSAEPLYGPQGLALTSDGHVVVADAGNHC 638
Cdd:COG4257   16 GSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFTEY---PLGGGSGPHGIAVDPDGNLWFTDNGNNR 81
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
535-644 6.01e-06

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.86  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  535 KNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVD-SNGNIIVADWGNSRIQVFD-SSGSFLSYINTSA 612
Cdd:pfam17170  53 DDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDkSNNSIYILDFMQNKILTYDlDGYSFIGEINLDL 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568951067  613 EP-----------LYGPQGLA--LTSDGHVVVADA-GNHCFKAYRY 644
Cdd:pfam17170 133 LPsdccqldkgklAFDSSGFDdgKRSGFYLVITDElGNIISGFFPA 178
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
400-559 6.51e-06

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 48.48  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  400 GRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDII-VADYDNRWVSIFSPEG-KFKTKigagrl 477
Cdd:pfam17170  54 DRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDKSNNSIyILDFMQNKILTYDLDGySFIGE------ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  478 mgpkgvavdrnghiIVVDNKSCCVFTFQPNgKLVgrFGGRGATDRHFAGPHFVAVNNKNEIVVTDF---------HNHSV 548
Cdd:pfam17170 128 --------------INLDLLPSDCCQLDKG-KLA--FDSSGFDDGKRSGFYLVITDELGNIISGFFpaeftlgilFNSSV 190
                         170
                  ....*....|.
gi 568951067  549 KVYSADGEFLF 559
Cdd:pfam17170 191 PFYEYGDNIYF 201
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
23-53 1.87e-05

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: 42.01  E-value: 1.87e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568951067  23 KTMEFYCEACETAMCGECR-AGEHREHGTVLL 53
Cdd:cd19756    8 EPLKLFCETCQELVCVLCLlSGEHRGHKVVPL 39
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
55-214 3.02e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    55 DVVEQHkAALQRQLEAVRGRLPQ----LSAAIALV---GGISQQLQERKAEALAQISAAFEDLEQALQQRKQA------L 121
Cdd:pfam01576  219 DLQEQI-AELQAQIAELRAQLAKkeeeLQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   122 VSDLESicgakqkvLQTQL-DTLrqgqehigsSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQL-E 199
Cdd:pfam01576  298 GEELEA--------LKTELeDTL---------DTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALeE 360
                          170
                   ....*....|....*
gi 568951067   200 LVLEVDGLRRSVLNL 214
Cdd:pfam01576  361 LTEQLEQAKRNKANL 375
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
435-462 3.70e-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: 40.85  E-value: 3.70e-05
                          10        20
                  ....*....|....*....|....*...
gi 568951067  435 LQRPTGVAVDTNGDIIVADYDNRWVSIF 462
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
23-61 5.82e-05

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: 40.77  E-value: 5.82e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568951067  23 KTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHK 61
Cdd:cd19769    8 KPLELFCRTDQMCICELCAKEEHRGHDVVTVEEEREKKE 46
YjiK COG3204
Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only];
432-627 6.44e-05

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


Pssm-ID: 442437 [Multi-domain]  Cd Length: 271  Bit Score: 44.96  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 432 PGQLQRPTGVA--VDTNGDIIVADyDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGK 509
Cdd:COG3204   45 PGELDEISGLTynPDTGTLFAVQD-EPGEIFELSLTGKVLRRIPLGGFGDYEGIAYLGDGRYVLVSEGTQTLYEVTLDDG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 510 lvGRFGGRGATDRHFAGPHfvaVNNKN-EIVVTDFHNHS---VK------VYSADGEFLFKFGSHGEGNGQFNAPTGVAV 579
Cdd:COG3204  124 --TTVLRADVKSLKLGLSE---KGNKGfEGLAYDPKNNRlfvAKerdpdgIYEFDLDSKKLTGSPDKALKGVKDPSALAI 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568951067 580 DS-NGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYG-PQGLALTSDG 627
Cdd:COG3204  199 DPiTGHLLILSDESKLLLELDRDGKVVSALSLDKGFDFPqPEGIAFDPDG 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
54-209 7.11e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 7.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   54 RDVVEQHKAAL-----QRQLEAVRGRLPQLSAAIAlvggisqQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESI 128
Cdd:COG4913   271 LAELEYLRAALrlwfaQRRLELLEAELEELRAELA-------RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  129 cGAKQKVLQTQLDTLRQGQEhigsscSFAEQALRLG-----SAPEVLLVRKHMRERLAALAAQafpERPHENAQLELVLE 203
Cdd:COG4913   344 -EREIERLERELEERERRRA------RLEALLAALGlplpaSAEEFAALRAEAAALLEALEEE---LEALEEALAEAEAA 413

                  ....*.
gi 568951067  204 VDGLRR 209
Cdd:COG4913   414 LRDLRR 419
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
388-415 7.50e-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: 40.08  E-value: 7.50e-05
                          10        20
                  ....*....|....*....|....*...
gi 568951067  388 FTNLQGVSAASSGRIVVADSNNQCIQVF 415
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
WD40 COG2319
WD40 repeat [General function prediction only];
426-632 8.43e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 426 GVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVV--DNKSCCVFT 503
Cdd:COG2319   69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASgsADGTVRLWD 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 504 FQpNGKLVGRFGGrgatdrHFAGPHFVAVNNKNEIVVTDFHNHSVKVYS-ADGEFLFKFGSHGegngqfNAPTGVAVDSN 582
Cdd:COG2319  149 LA-TGKLLRTLTG------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTLTGHT------GAVRSVAFSPD 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568951067 583 GNIIVADWGNSRIQVFD-SSGSFLSYINTSAEPLYgpqGLALTSDGHVVVA 632
Cdd:COG2319  216 GKLLASGSADGTVRLWDlATGKLLRTLTGHSGSVR---SVAFSPDGRLLAS 263
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
371-415 1.15e-04

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: 44.46  E-value: 1.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568951067 371 EDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVF 415
Cdd:cd14954  241 DGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
615-642 1.17e-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: 39.31  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*...
gi 568951067  615 LYGPQGLALTSDGHVVVADAGNHCFKAY 642
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 ...
27-56 2.55e-04

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: 38.94  E-value: 2.55e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 568951067  27 FYCEACETAMCGECRAGEHREHGTVLLRDV 56
Cdd:cd19785   14 LFCETCDKPVCRDCVLVEHRGHQCDFTSDV 43
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
57-209 4.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  57 VEQHKAALQRQLEAVRGRLPQ----LSAAIALVGGISQQLQERKAEAlAQISAAFEDLE---QALQQRKQAL---VSDLE 126
Cdd:COG4372   64 LEEELEQARSELEQLEEELEElneqLQAAQAELAQAQEELESLQEEA-EELQEELEELQkerQDLEQQRKQLeaqIAELQ 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 127 SICGAKQKvlqtQLDTLRQGQEHIgsscsfAEQALRLGSAPEVLLVRKHmRERLAALAAQAFPERPHENAQLELVLEVDG 206
Cdd:COG4372  143 SEIAEREE----ELKELEEQLESL------QEELAALEQELQALSEAEA-EQALDELLKEANRNAEKEEELAEAEKLIES 211

                 ...
gi 568951067 207 LRR 209
Cdd:COG4372  212 LPR 214
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
44-163 4.28e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    44 EHREHGTVLLRD----VVEQHKAALQRQLEAVRGRLPQLSAAIAlvggisQQLQERKAEALAQISAAfedleQALQQRKQ 119
Cdd:TIGR00618  405 LQREQATIDTRTsafrDLQGQLAHAKKQQELQQRYAELCAAAIT------CTAQCEKLEKIHLQESA-----QSLKEREQ 473
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568951067   120 ALvSDLESICgakQKVLQTQLDTLRQGQEHIGSSCSFAEQALRL 163
Cdd:TIGR00618  474 QL-QTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
513-637 5.42e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 43.30  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  513 RFGGRGATDRhFAGPHFVAVNNKNEIVVTDFhnhsvkvysaDGEFLFKFGSHGE--------GNGQFNAPTGVAVDSNGN 584
Cdd:PLN02919  568 KFPGKLAIDL-LNNRLFISDSNHNRIVVTDL----------DGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKN 636
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951067  585 II-VA----------DWGNSRIQVFDSSGS----FLSYINTSAEPLYGPQGLALTS-DGHVVVADAGNH 637
Cdd:PLN02919  637 LLyVAdtenhalreiDFVNETVRTLAGNGTkgsdYQGGKKGTSQVLNSPWDVCFEPvNEKVYIAMAGQH 705
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
43-225 7.94e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   43 GEHREHGT--------VLLRDVVEQhKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKA--EALAQISAAFEDLEQ 112
Cdd:COG4913   587 GTRHEKDDrrrirsryVLGFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVAS 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  113 A------LQQRKQAL---VSDLESIcGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQAL------------RLGSAPEvlL 171
Cdd:COG4913   666 AereiaeLEAELERLdasSDDLAAL-EEQLEELEAELEELEEELDELKGEIGRLEKELeqaeeeldelqdRLEAAED--L 742
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568951067  172 VRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSATAH 225
Cdd:COG4913   743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-304 8.73e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  54 RDVVEQHKAALQRQLEAVRGRLPQLSAAIAlvggisqQLQERKAEALAQISAAFEDLEQALQQRKQALvSDLESICGAKQ 133
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELE-------ELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELA 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 134 KVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRER--------LAALAAQAFPERPHENAQLELVLEVD 205
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEeleeleeaLAELEEEEEEEEEALEEAAEEEAELE 455
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 206 GLRRSVLN-LGALLTTSATAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELcaeITGPDGVRLAVPVVDHK 284
Cdd:COG1196  456 EEEEALLElLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGV 532
                        250       260
                 ....*....|....*....|
gi 568951067 285 NGTYELVYTARTEGDLLLSV 304
Cdd:COG1196  533 EAAYEAALEAALAAALQNIV 552
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
34-203 9.91e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   34 TAMCGECRAGEHREHGTVLLRDVVEQhKAALQRqLEAVRGRLPQLSAAIAlvggiSQQLQERKAEALAQISA----AFED 109
Cdd:COG3096   482 CKIAGEVERSQAWQTARELLRRYRSQ-QALAQR-LQQLRAQLAELEQRLR-----QQQNAERLLEEFCQRIGqqldAAEE 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  110 LEqALQQRKQALVSDLE---SICGAKQKVLQTQLDTLRQGQEhigsscSFAEQALRLGSAPEVLlvrkhmrERLAALAAQ 186
Cdd:COG3096   555 LE-ELLAELEAQLEELEeqaAEAVEQRSELRQQLEQLRARIK------ELAARAPAWLAAQDAL-------ERLREQSGE 620
                         170
                  ....*....|....*..
gi 568951067  187 AFPERPHENAQLELVLE 203
Cdd:COG3096   621 ALADSQEVTAAMQQLLE 637
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
477-504 1.53e-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: 1.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 568951067  477 LMGPKGVAVDRNGHIIVVDNKSCCVFTF 504
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
52-216 1.54e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   52 LLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQalvsdlesicga 131
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER------------ 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  132 KQKVLQTQLDTLrqGQEHIGSSCSFAEQALRLGSAPEVLLVRKH-MRERLAALAAQafpERPHENAQLELVLEVDGLRRS 210
Cdd:COG4913   360 RRARLEALLAAL--GLPLPASAEEFAALRAEAAALLEALEEELEaLEEALAEAEAA---LRDLRRELRELEAEIASLERR 434

                  ....*.
gi 568951067  211 VLNLGA 216
Cdd:COG4913   435 KSNIPA 440
Bbox2_TIF1g_C-VI cd19830
B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); ...
18-61 1.63e-03

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: 36.96  E-value: 1.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568951067  18 PAPTMKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHK 61
Cdd:cd19830   10 PVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQK 53
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
573-602 1.81e-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: 40.32  E-value: 1.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568951067  573 APTGVAVDSNGNIIVADWGNSRIQVFDSSG 602
Cdd:pfam08450 185 RPDGMAVDAEGNVWVARWGGGKVVRFDPDG 214
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
361-456 1.93e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 41.38  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  361 TGGKR---KDNPIEDELVFRVGSRGREKGE--FTNLQGVSAASSGRIVVADSNNQCIQVF----------SNEGQFKFRF 425
Cdd:PLN02919  771 TGGSRllaGGDPTFSDNLFKFGDHDGVGSEvlLQHPLGVLCAKDGQIYVADSYNHKIKKLdpatkrvttlAGTGKAGFKD 850
                          90       100       110
                  ....*....|....*....|....*....|.
gi 568951067  426 GvRGRSpGQLQRPTGVAVDTNGDIIVADYDN 456
Cdd:PLN02919  851 G-KALK-AQLSEPAGLALGENGRLFVADTNN 879
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
393-495 2.46e-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: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 393 GVSAASSGRIVVADSNNQCIQVFS-NEGQFK------------FRFGVRGRSPGQ--LQRPTGVAVDTNGDIIVADYDN- 456
Cdd:cd14951  138 GLSLAGWGELFVADSESSAIRAVSlKDGGVKtlvggtrvgtglFDFGDRDGPGAEalLQHPLGVAALPDGSVYVADTYNh 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568951067 457 ---RW------VSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVD 495
Cdd:cd14951  218 kikRVdpatgeVSTLAGTGKAGYKDLEAQFSEPSGLVVDGDGRLYVAD 265
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
53-145 2.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  53 LRDVVEQhKAALQRQLEAVRGRLPQLSAAIAlvgGISQQLQERKAEalaqisaaFEDLEQALQQRKQALVSDLESICGAK 132
Cdd:COG4372   33 LRKALFE-LDKLQEELEQLREELEQAREELE---QLEEELEQARSE--------LEQLEEELEELNEQLQAAQAELAQAQ 100
                         90
                 ....*....|....*
gi 568951067 133 Q--KVLQTQLDTLRQ 145
Cdd:COG4372  101 EelESLQEEAEELQE 115
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
342-415 2.49e-03

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: 40.26  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 342 GPGSHVRQK--AVRRPSSMYSTGGKrKDNPI----EDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVF 415
Cdd:cd14962  190 GPGSFARPKgiAVDSEGNIYVVDAA-FDNVQifnpEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRRIQVF 268
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-238 2.95e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067    57 VEQHKAALQRQLEAVRGRLPQLSAAIALVggisQQLQERKAEALAQISAAFEDLE------QALQQRKQALVSDLESICG 130
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKeeleslEAELEELEAELEELESRLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   131 AKQKVLQTQLDTLRQGQEHIgsscsfAEQALRLGSAPEVLLVRKHMRERLAALAAQAfPERPHENAQLELVLEVDGLRRs 210
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQI------ASLNNEIERLEARLERLEDRRERLQQEIEEL-LKKLEEAELKELQAELEELEE- 447
                          170       180
                   ....*....|....*....|....*...
gi 568951067   211 vlnlgALLTTSATAHETVATGEGLRQAL 238
Cdd:TIGR02168  448 -----ELEELQEELERLEEALEELREEL 470
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
513-599 4.57e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 40.22  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  513 RFGGRG--ATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVY----------SADGEFLFKFGSHGEGngQFNAPTGVAVD 580
Cdd:PLN02919  790 KFGDHDgvGSEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLdpatkrvttlAGTGKAGFKDGKALKA--QLSEPAGLALG 867
                          90
                  ....*....|....*....
gi 568951067  581 SNGNIIVADWGNSRIQVFD 599
Cdd:PLN02919  868 ENGRLFVADTNNSLIRYLD 886
Bbox2_TIF1_C-VI cd19775
B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This ...
25-49 6.09e-03

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: 35.00  E-value: 6.09e-03
                         10        20
                 ....*....|....*....|....*
gi 568951067  25 MEFYCEACETAMCGECRAGEHREHG 49
Cdd:cd19775   12 LKLFCETCDKLTCRDCQLLEHKDHK 36
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
443-607 6.17e-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: 39.23  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  443 VDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAgRLMGP------KGVAVDR-NGHIIVVDNKSCCVFTFqpngklvgrfg 515
Cdd:pfam17170  50 KFVDDRIFVFDSNTNNLFVFDKKGKFVRQIGA-QGNGPgeylqiNDFIIDKsNNSIYILDFMQNKILTY----------- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  516 grGATDRHFAGphfvavnnknEIVVTDFHNHsvkVYSADGEFLFkFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRI 595
Cdd:pfam17170 118 --DLDGYSFIG----------EINLDLLPSD---CCQLDKGKLA-FDSSGFDDGKRSGFYLVITDELGNIISGFFPAEFT 181
                         170
                  ....*....|....
gi 568951067  596 Q--VFDSSGSFLSY 607
Cdd:pfam17170 182 LgiLFNSSVPFYEY 195
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
57-121 6.24e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 36.91  E-value: 6.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568951067   57 VEQHKAaLQRQLEAVRGRLPQLSAaialvggISQQLQERKAEA-------LAQISAAFEDLEQALQQRKQAL 121
Cdd:pfam00435  40 LKKHKA-LEAELAAHQDRVEALNE-------LAEKLIDEGHYAseeiqerLEELNERWEQLLELAAERKQKL 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
58-226 7.43e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  58 EQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQA------LQQRKQALVSDLESICGA 131
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeleeLEEELEEAEEELEEAEAE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067 132 KQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVR-KHMRERLAALAAQAfpERpHENAQLELVLEVDGLRRS 210
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQlEELEEAEEALLERL--ER-LEEELEELEEALAELEEE 436
                        170
                 ....*....|....*.
gi 568951067 211 VLNLGALLTTSATAHE 226
Cdd:COG1196  437 EEEEEEALEEAAEEEA 452
Bbox2_TIF1a_C-VI cd19828
B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); ...
18-64 7.72e-03

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: 35.02  E-value: 7.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568951067  18 PAPTMKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAAL 64
Cdd:cd19828    7 PFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVII 53
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
50-131 7.82e-03

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 39.06  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  50 TVLLRDV----VEQHKAALQRQLE--AVRGRLPQlSAAIALVGGIS--QQLQERKAEALAqISAAFEDLEQalqqrKQAL 121
Cdd:PRK08268  32 TVLLYDAragaAAAARDGIAARLAklVEKGKLTA-EQADAALARLRpvEALADLADCDLV-VEAIVERLDV-----KQAL 104
                         90
                 ....*....|
gi 568951067 122 VSDLESICGA 131
Cdd:PRK08268 105 FAQLEAIVSP 114
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
54-199 8.09e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.40  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   54 RDVVEQHKAALQRQLEAVRGRLPQLSaaialvggisQQLQERKAEAlaqisaafedleQALQQRKQALVSDLESICGAKQ 133
Cdd:PRK10246  532 LDALEKEVKKLGEEGAALRGQLDALT----------KQLQRDESEA------------QSLRQEEQALTQQWQAVCASLN 589
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951067  134 KVLQTQLDT---LRQGQEHigsscsfaEQALRlgsapevLLVRKHMRErlAALAAQAFPERPHEnAQLE 199
Cdd:PRK10246  590 ITLQPQDDIqpwLDAQEEH--------ERQLR-------LLSQRHELQ--GQIAAHNQQIIQYQ-QQIE 640
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
54-214 9.25e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.44  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067   54 RDVVEQHKAALQRQLEAVRGRLPQLSAAIAlvggisqQLQERKAEALAQISAA--FEDLEQALQQRKQALVSDLESICGA 131
Cdd:pfam12795  32 IDASKQRAAAYQKALDDAPAELRELRQELA-------ALQAKAEAAPKEILASlsLEELEQRLLQTSAQLQELQNQLAQL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951067  132 KQKV--LQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLV---RKHMRERLAALAAQafperpheNAQLELVLEVDG 206
Cdd:pfam12795 105 NSQLieLQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSeaqRWALQAELAALKAQ--------IDMLEQELLSNN 176

                  ....*...
gi 568951067  207 LRRSVLNL 214
Cdd:pfam12795 177 NRQDLLKA 184
 
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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