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Conserved domains on  [gi|1034639127|ref|XP_016863442|]
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tripartite motif-containing protein 2 isoform X6 [Homo sapiens]

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; ...
346-623 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: 578.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAgtldGPH 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFA----GPH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 506 FAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI 585
Cdd:cd14960   157 FAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034639127 586 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 623
Cdd:cd14960   237 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 6.75e-36

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


:

Pssm-ID: 128778  Cd Length: 127  Bit Score: 130.85  E-value: 6.75e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639127  116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQ 162
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
200-296 1.95e-24

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: 97.67  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1034639127  280 LRLYDQHIRGSPFKLKV 296
Cdd:smart00557  74 VKFGGEHIPGSPFTVKV 90
Bbox_SF super family cl00034
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
1-31 5.28e-20

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 cd19824:

Pssm-ID: 469587 [Multi-domain]  Cd Length: 42  Bit Score: 83.18  E-value: 5.28e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKD 31
Cdd:cd19824    12 MEFYCQSCETAMCQECTEGEHAEHPTVPLKD 42
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
346-623 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: 578.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAgtldGPH 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFA----GPH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 506 FAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI 585
Cdd:cd14960   157 FAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034639127 586 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 623
Cdd:cd14960   237 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 6.75e-36

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 130.85  E-value: 6.75e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639127  116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQ 162
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-621 1.28e-28

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 115.12  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRfgirgrSPGQLQRPTGVAVHPSGDIIIADY-DNKWVSIFS 436
Cdd:COG4257    14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFTEY------PLGGGSGPHGIAVDPDGNLWFTDNgNNRIGRIDP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP-NGKIVTRFGSRGNGdrqfagtldGPHFAAVNSNNEI 515
Cdd:COG4257    88 KTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPaTGEVTEFPLPTGGA---------GPYGIAVDPDGNL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 516 IITDFHNHSVKVFNQEGEFMLKFgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-GSGSFLSYinTSADPLYG 594
Cdd:COG4257   159 WVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGAR 232
                         250       260
                  ....*....|....*....|....*..
gi 1034639127 595 PQGLALTSDGHVVVADSGNHcfKVYRY 621
Cdd:COG4257   233 PYGVAVDGDGRVWFAESGAN--RIVRF 257
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
36-157 9.75e-27

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: 104.93  E-value: 9.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034639127 116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLN 157
Cdd:cd20482    81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARLQ 122
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
200-296 1.95e-24

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: 97.67  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1034639127  280 LRLYDQHIRGSPFKLKV 296
Cdd:smart00557  74 VKFGGEHIPGSPFTVKV 90
Filamin pfam00630
Filamin/ABP280 repeat;
200-293 1.66e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 200 ASETVATGEGLRQTIIGQPMSVTITTKDKDGELcktgnaylTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 1034639127 280 LRLYDQHIRGSPFK 293
Cdd:pfam00630  76 VKFNGQHIPGSPFK 89
Bbox2_TRIM2_C-VII cd19824
B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar ...
1-31 5.28e-20

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: 83.18  E-value: 5.28e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKD 31
Cdd:cd19824    12 MEFYCQSCETAMCQECTEGEHAEHPTVPLKD 42
BBOX smart00336
B-Box-type zinc finger;
1-29 1.30e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.88  E-value: 1.30e-09
                           10        20
                   ....*....|....*....|....*....
gi 1034639127    1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:smart00336  14 AEFFCEECGALLCRTCDEAEHRGHTVVLL 42
zf-B_box pfam00643
B-box zinc finger;
1-29 3.69e-08

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 49.78  E-value: 3.69e-08
                          10        20
                  ....*....|....*....|....*....
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:pfam00643  14 LTLYCNDCQELLCEECSVGEHRGHTVVPL 42
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
548-575 1.45e-07

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 47.78  E-value: 1.45e-07
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 548 FNAPTGVAVDSNGNIIVADWGNSRIQVF 575
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
361-576 1.39e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 48.31  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  361 FTNLQGVAASTNGKIL-IADSNN----------QCVQIFSNDGQFKSRFgiRGRSPGQLQ---RPTGVAVHPSGDII--- 423
Cdd:PLN02919   623 FNRPQGLAYNAKKNLLyVADTENhalreidfvnETVRTLAGNGTKGSDY--QGGKKGTSQvlnSPWDVCFEPVNEKVyia 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  424 ------IADYD--NKWVSIFSSDGKFKTKIGSG----KLMGPKGVSVDRN-GHIIVVDNKACCVFIFQpngkiVTRFGSR 490
Cdd:PLN02919   701 magqhqIWEYNisDGVTRVFSGDGYERNLNGSSgtstSFAQPSGISLSPDlKELYIADSESSSIRALD-----LKTGGSR 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  491 --GNGDRQFAGTL------DGP-------HFAAV--NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGN-------- 545
Cdd:PLN02919   776 llAGGDPTFSDNLfkfgdhDGVgsevllqHPLGVlcAKDGQIYVADSYNHKIKKLDPATKRVTTLAGTGKAGfkdgkalk 855
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034639127  546 GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 576
Cdd:PLN02919   856 AQLSEPAGLALGENGRLFVADTNNSLIRYLD 886
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
34-190 2.91e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.12  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  34 EQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHstfdELQKTLNVRksvllmELEVNyGLKHKV-- 111
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR----DLKDMLDVK------ERKIN-VLQKKIen 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 112 LQSQL---DTLLQG-QESIKSC---SNFTAQALnhGTETEVLLVKKQMSEKLNEladqdfplhPRENDQLDFIVETEGLK 184
Cdd:pfam10174 406 LQEQLrdkDKQLAGlKERVKSLqtdSSNTDTAL--TTLEEALSEKERIIERLKE---------QREREDRERLEELESLK 474

                  ....*.
gi 1034639127 185 KSIHNL 190
Cdd:pfam10174 475 KENKDL 480
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
548-609 5.20e-04

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


Pssm-ID: 467996 [Multi-domain]  Cd Length: 330  Bit Score: 42.65  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639127 548 FNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSfLSYI------NTSADPLYGPQGLALTSDGHVVVA 609
Cdd:NF033206  249 FTGLTDLAFDPDGNLYVLELAGGGLLKGDPTGS-LIRIapdgtrTTLLDGLELPTGLAVGPDGTLYVT 315
 
Name Accession Description Interval E-value
NHL_TRIM2_like cd14960
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ...
346-623 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: 578.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAgtldGPH 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFA----GPH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 506 FAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI 585
Cdd:cd14960   157 FAAVNNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYI 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034639127 586 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 623
Cdd:cd14960   237 NTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
355-619 1.37e-94

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: 291.53  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 355 GRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSI 434
Cdd:cd05819     1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFNEPAGVAVDSDGNLYVADTGNHRIQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 435 FSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFagtlDGPHFAAV 509
Cdd:cd05819    81 FDPDGNFLASFGGsgdgdGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGSGGSGPGQF----NGPTGVAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 510 NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS---YIN 586
Cdd:cd05819   157 DSDGNIYVADTGNHRIQVFDPDGNFLTTFGSTGTGPGQFNYPTGIAVDSDGNIYVADSGNNRVQVFDPDGAGFGgngNFL 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034639127 587 TSADPLYGPQGLALTSDGHVVVADSGNHCFKVY 619
Cdd:cd05819   237 GSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
347-619 9.06e-90

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: 279.82  E-value: 9.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 347 LIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIAD 426
Cdd:cd14954     9 PLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRDGQFDRPAGVAVNSRGRIIVAD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 427 YDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFagtl 501
Cdd:cd14954    89 KDNHRIQVFDLNGRFLLKFGErgtknGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPGQL---- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 502 DGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSF 581
Cdd:cd14954   165 DSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEF 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034639127 582 LSYINT---SADPLYGPQGLALTSDGHVVVADSGNHCFKVY 619
Cdd:cd14954   245 LCSFGTegnGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
352-615 3.71e-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: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 249.42  E-value: 3.71e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14955     6 GSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVADTGNHR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFagtlDGPHF 506
Cdd:cd14955    86 IQKFDSTGTFLTKWGSsgsgdGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQF----NSPTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 507 AAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS--- 583
Cdd:cd14955   162 IAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVDSAGNVYVADTGNNRIQKFDSSGTFITkwg 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034639127 584 YINTSADPLYGPQGLALTSDGHVVVADSGNHC 615
Cdd:cd14955   242 SEGSGDGQFNSPSGIAVDSAGNVYVADSGNNR 273
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
345-620 4.09e-70

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: 228.30  E-value: 4.09e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 345 DDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIII 424
Cdd:cd14957     1 ASFSYAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYSYSIGSGGTGSGQFNSPYGIAVDSNGNIYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 425 ADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFag 499
Cdd:cd14957    81 ADTDNNRIQVFNSSGVYQYSIGTggsgdGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTSSGTFSYSIGSGGTGPGQF-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 500 tlDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSG 579
Cdd:cd14957   159 --NGPQGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSG 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034639127 580 SFLSYINTSADPLYG---PQGLALTSDGHVVVADSGNHCFKVYR 620
Cdd:cd14957   237 AYQYSIGTSGSGNGQfnyPYGIAVDNDGKIYVADSNNNRIQVFN 280
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
352-614 8.80e-68

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: 222.16  E-value: 8.80e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14956     3 GGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGdrqfAGTLDGPHF 506
Cdd:cd14956    83 IQVFTLTGELQTIGGSsgsgpGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIE----PGSFNYPRG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 507 AAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYIN 586
Cdd:cd14956   159 VAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWG 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034639127 587 TSAD---PLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14956   239 SPGTgpgQFKNPWGVVVDADGTVYVADSNNN 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
388-614 8.63e-62

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: 206.63  E-value: 8.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 388 FSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNG 462
Cdd:cd14954     3 YRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSygsrdGQFDRPAGVAVNSRG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 463 HIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFagtlDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNG 542
Cdd:cd14954    83 RIIVADKDNHRIQVFDLNGRFLLKFGERGTKNGQF----NYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEG 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034639127 543 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSAD---PLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14954   159 AGPGQLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSgngQFKRPRGVAVDDEGNIIVADSGNH 233
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
352-620 7.35e-59

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: 198.27  E-value: 7.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14961     1 GSFGGWPGTLNNPTGVAVTPTGRVVVADDGNKRIQVFDSDGNCLQQFGPKGDAGQDIRYPLDVAVTPDGHIVVTDAGDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 432 VSIFSSDGKFKTKIGSGKLMgPKGVSVDRNGHIIVVDNKACCVFIFQ---PNGKIVTRFGSRGNgdrqfagtLDGPHFAA 508
Cdd:cd14961    81 VKVFSFDGRLKLFVRKSFSL-PWGVAVNPSGEILVTDSEAGKLFVLTvdfKLGILKKGQKLCSQ--------LCRPRFVA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 509 VNSNNEIIITD--------FHNHSVKVFNQEGEF---MLKFGsNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDG 577
Cdd:cd14961   152 VSRLGAVAVTEhlfangtrSSSTRVKVFSSGGQLlgqIDSFG-LNLVFPSLICASGVAFDSEGNVIVADTGSGAILCLGK 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034639127 578 SGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYR 620
Cdd:cd14961   231 PEGFPILKPIVTQGLSRPVGLAVTPDGSLVVLDSGNHCVKIYK 273
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
394-614 1.11e-55

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


Pssm-ID: 271325 [Multi-domain]  Cd Length: 279  Bit Score: 190.10  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 394 FKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVD 468
Cdd:cd14955     1 FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSsgsgdGQFYSPTGIAVDSDGNVYVAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 469 NKACCVFIFQPNGKIVTRFGSRGNGDRQFagtlDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQF 548
Cdd:cd14955    81 TGNHRIQKFDSTGTFLTKWGSSGSGDGQF----NSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639127 549 NAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTS---ADPLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14955   157 NSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEgsgDGQFNAPYGIAVDSAGNVYVADTGNN 225
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
346-622 1.42e-53

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: 184.40  E-value: 1.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 346 DLIFR--VGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAV-HPSGDI 422
Cdd:cd14959     4 KMIIHckFGESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQVFDKEGEFKFQFGIPGKRDGQLWYPNKVAVcRVTGRY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 423 IIADYDNK--WVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSrgngdrqfAGT 500
Cdd:cd14959    84 VVTDRGNPrhRMQIFTKRGQFVRKFGARYLQHVRGLTVDAAGHIIVVESKVMRVFIFDESGNVLKWFDC--------SKY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 501 LDGPHFAAVNsNNEIIITDFHNHSVKVFNQEGEFMLKFGsngeGNGQFNAPTGVAVDSNGNIIVADWGNSR--IQVFDGS 578
Cdd:cd14959   156 LEEPSDVAVN-DNEIYICDNKGHCVVVFNYDGQFLRRIG----GEGITNYPIGVDISSAGDVLVADNHGNHfhVTVFTRD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034639127 579 GSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYL 622
Cdd:cd14959   231 GQLISEFECPRVKHSRCCGLALTSEGSIVTLSKHNHHVLVFNTL 274
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
366-619 4.61e-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: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 180.18  E-value: 4.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 366 GVAAStNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKI 445
Cdd:cd14963    14 GVAVS-DGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKYF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 446 GSGK----LMGPKGVSVDRnGHIIVVDNKACCVFIFQPNGKIVTRFGSRGngdrQFAGTLDGPHFAAVNSNNEIIITDFH 521
Cdd:cd14963    93 PEKKdrvkLISPAGLAIDD-GKLYVSDVKKHKVIVFDLEGKLLLEFGKPG----SEPGELSYPNGIAVDEDGNIYVADSG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 522 NHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSAD---PLYGPQGL 598
Cdd:cd14963   168 NGRIQVFDKNGKFIKELNGSPDGKSGFVNPRGIAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKddgQFNLPNGL 247
                         250       260
                  ....*....|....*....|.
gi 1034639127 599 ALTSDGHVVVADSGNHCFKVY 619
Cdd:cd14963   248 FIDDDGRLYVTDRENNRVAVY 268
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
398-620 3.79e-51

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 177.86  E-value: 3.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 398 FGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKAC 472
Cdd:cd14956     2 WGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTtgdgpGQFGRPRGLAVDKDGWLYVADYWGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 473 CVFIFQPNGKIVTRFGSRGNGDRQFagtlDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPT 552
Cdd:cd14956    82 RIQVFTLTGELQTIGGSSGSGPGQF----NAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIEPGSFNYPR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639127 553 GVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTS-ADP--LYGPQGLALTSDGHVVVADSGNHCFKVYR 620
Cdd:cd14956   158 GVAVDPDGTLYVADTYNDRIQVFDNDGAFLRKWGGRgTGPgqFNYPYGIAIDPDGNVFVADFGNNRIQKFT 228
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
365-622 6.09e-51

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


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 177.01  E-value: 6.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 365 QGVAASTNGKILIADSNNQCVQIFsnDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTK 444
Cdd:cd14962    15 YGVAADGRGRIYVADTGRGAVFVF--DLPNGKVFVIGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 445 IGSGKLMG-PKGVSVD-RNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGtldgPHFAAVNSNNEIIITDFHN 522
Cdd:cd14962    93 IGAGALFKrPTGIAVDpAGKRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNL----PTDLAVDRDGNLYVTDTMN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 523 HSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI-NTSADP--LYGPQGLA 599
Cdd:cd14962   169 FRVQIFDADGKFLRSFGERGDGPGSFARPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVgGPGSGPgeFYLPSGIA 248
                         250       260
                  ....*....|....*....|...
gi 1034639127 600 LTSDGHVVVADSGNHCFKVYRYL 622
Cdd:cd14962   249 IDKDDRIYVVDQFNRRIQVFQYL 271
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
348-575 1.41e-44

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: 159.76  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 348 IFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGiRGRSPGQLQRPTGVAVHpSGDIIIADY 427
Cdd:cd14963    42 KKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKYFP-EKKDRVKLISPAGLAID-DGKLYVSDV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 428 DNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAgtld 502
Cdd:cd14963   120 KKHKVIVFDLEGKLLLEFGKpgsepGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKELNGSPDGKSGFV---- 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 503 GPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 575
Cdd:cd14963   196 NPRGIAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
350-575 2.31e-41

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: 151.20  E-value: 2.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 350 RVGTKGRNKGE-FTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGirgrSPGQLQRPTGVAVHPSGD-IIIADY 427
Cdd:cd14962    44 KVFVIGNAGPNrFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRAIG----AGALFKRPTGIAVDPAGKrLYVVDT 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 428 DNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAgtld 502
Cdd:cd14962   120 LAHKVKVFDLDGRLLFDIGKrgsgpGEFNLPTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGERGDGPGSFA---- 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 503 GPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 575
Cdd:cd14962   196 RPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRRIQVF 268
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
361-614 1.32e-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: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 361 FTNLQGVAASTNGKILIADSNNQCVQIFSNDGQfKSRF---GIRGRSPG-----QLQRPTGVAVHPSGDIIIADYDNKWV 432
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKITPDGV-VTTVagtGTAGFADGggaaaQFNTPSGVAVDAAGNLYVADTGNHRI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 433 SIFSSDGKFKTKIGSG-------------KLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVT-----RFGSRGNGD 494
Cdd:cd14953   101 RKITPDGVVSTLAGTGtagfsddggataaQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVTTvagtgGAGYAGDGP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 495 RQFAgTLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEG--------NGQFNAPTGVAVDSNGNIIVAD 566
Cdd:cd14953   181 ATAA-QFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGTAGfsgdggatAAQLNNPTGVAVDAAGNLYVAD 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639127 567 WGNSRI----------QVFDGSGSFLSYINTSAD-PLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14953   260 SGNHRIrkitpagvvtTVAGGGAGFSGDGGPATSaQFNNPTGVAVDAAGNLYVADTGNN 318
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 6.75e-36

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 130.85  E-value: 6.75e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034639127  116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQ 162
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
405-613 3.39e-33

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: 129.31  E-value: 3.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 405 PGQLQRPTGVAVHPSGDIII-ADYDNKWVS--------------------IFSSDGKFKTKIGSGKLMGPKGVSVDRNGH 463
Cdd:cd14958     9 SLKLGQVSGVAVDSLGNGVVfHRGGRVWDAnsfdanvyvfkgpieedtilVFDPDGGFLRSWGAGLFYMPHGLTIDPDGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 464 IIVVDNKACCVFIFQPNGKIVTRFGSrgnGDRQFAGTlDGPHFA-----AVNSNNEIIITDFH-NHSVKVFNQEGEFMLK 537
Cdd:cd14958    89 IWVTDVGLHQVFKFDPEGKLLPLLTL---GERGEPGS-DQTHFCkptdvAVAPDGDIFVADGYcNSRIVKFSPDGKLLKS 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639127 538 FGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS-YINTSADPLYgpqGLALTSDGHVVVADSGN 613
Cdd:cd14958   165 WGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLTeWTNPELGRPY---ALAIDPDGLLYVVDGPP 238
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
407-615 5.39e-29

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: 117.63  E-value: 5.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 407 QLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSG------------KLMGPKGVSVDRNGHIIVVDNKACCV 474
Cdd:cd14953    21 RFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGtagfadgggaaaQFNTPSGVAVDAAGNLYVADTGNHRI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 475 FIFQPNGKIVT------RFGSRGNGDRqfAGTLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFM-----LKFGSNGE 543
Cdd:cd14953   101 RKITPDGVVSTlagtgtAGFSDDGGAT--AAQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVTtvagtGGAGYAGD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 544 GNG---QFNAPTGVAVDSNGNIIVADWGNSRIQVFD---------GSGSFLS---YINTSAdPLYGPQGLALTSDGHVVV 608
Cdd:cd14953   179 GPAtaaQFNNPTGVAVDAAGNLYVADRGNHRIRKITpdgvvttvaGTGTAGFsgdGGATAA-QLNNPTGVAVDAAGNLYV 257

                  ....*..
gi 1034639127 609 ADSGNHC 615
Cdd:cd14953   258 ADSGNHR 264
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-621 1.28e-28

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 115.12  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRfgirgrSPGQLQRPTGVAVHPSGDIIIADY-DNKWVSIFS 436
Cdd:COG4257    14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFTEY------PLGGGSGPHGIAVDPDGNLWFTDNgNNRIGRIDP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP-NGKIVTRFGSRGNGdrqfagtldGPHFAAVNSNNEI 515
Cdd:COG4257    88 KTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPaTGEVTEFPLPTGGA---------GPYGIAVDPDGNL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 516 IITDFHNHSVKVFNQEGEFMLKFgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-GSGSFLSYinTSADPLYG 594
Cdd:COG4257   159 WVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGAR 232
                         250       260
                  ....*....|....*....|....*..
gi 1034639127 595 PQGLALTSDGHVVVADSGNHcfKVYRY 621
Cdd:COG4257   233 PYGVAVDGDGRVWFAESGAN--RIVRF 257
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
497-619 4.09e-27

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: 110.84  E-value: 4.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 497 FAGTLDGPHFAAVnSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 576
Cdd:cd14963     5 FGDPLNKPMGVAV-SDGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034639127 577 GSGSFLSYINTSAD--PLYGPQGLALtSDGHVVVADSGNHCFKVY 619
Cdd:cd14963    84 PDGKFLKYFPEKKDrvKLISPAGLAI-DDGKLYVSDVKKHKVIVF 127
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
352-572 8.40e-27

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: 111.47  E-value: 8.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKG-----EFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFkSRF---GIRGRSPG------QLQRPTGVAVH 417
Cdd:cd14953    62 GTAGFADGggaaaQFNTPSGVAVDAAGNLYVADTGNHRIRKITPDGVV-STLagtGTAGFSDDggataaQFNYPTGVAVD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 418 PSGDIIIADYDNKWVSIFSSDGKFKTKIGSG-------------KLMGPKGVSVDRNGHIIVVD---NKACCVFifqPNG 481
Cdd:cd14953   141 AAGNLYVADTGNHRIRKITPDGVVTTVAGTGgagyagdgpataaQFNNPTGVAVDAAGNLYVADrgnHRIRKIT---PDG 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 482 KIVTRFGSRGNGDRQFAG----TLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFM----LKFGSNGEGNG----QFN 549
Cdd:cd14953   218 VVTTVAGTGTAGFSGDGGataaQLNNPTGVAVDAAGNLYVADSGNHRIRKITPAGVVTtvagGGAGFSGDGGPatsaQFN 297
                         250       260
                  ....*....|....*....|...
gi 1034639127 550 APTGVAVDSNGNIIVADWGNSRI 572
Cdd:cd14953   298 NPTGVAVDAAGNLYVADTGNNRI 320
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
405-621 9.54e-27

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 109.72  E-value: 9.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 405 PGQLQRPTGVAVHPSGDIIIADYDNKWVSIFS-SDGKFkTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKI 483
Cdd:COG4257    13 PAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEF-TEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 484 VTRFGSRGNGdrqfagtlDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGqfnaPTGVAVDSNGNII 563
Cdd:COG4257    92 ITTFALPGGG--------SNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPLPTGGAG----PYGIAVDPDGNLW 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639127 564 VADWGNSRIQVFDGSGSFLSYINTSAdPLYGPQGLALTSDGHVVVADSGNHcfKVYRY 621
Cdd:COG4257   160 VTDFGANAIGRIDPDTGTLTEYALPT-PGAGPRGLAVDPDGNLWVADTGSG--RIGRF 214
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
36-157 9.75e-27

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: 104.93  E-value: 9.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034639127 116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLN 157
Cdd:cd20482    81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARLQ 122
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
352-479 6.23e-26

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: 107.66  E-value: 6.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14955   147 GSFGSGDGQFNSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVDSAGNVYVADTGNNR 226
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP 479
Cdd:cd14955   227 IQKFDSSGTFITKWGSegsgdGQFNSPSGIAVDSAGNVYVADSGNNRIQKFAP 279
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
200-296 1.95e-24

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: 97.67  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1034639127  280 LRLYDQHIRGSPFKLKV 296
Cdd:smart00557  74 VKFGGEHIPGSPFTVKV 90
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
361-614 1.20e-22

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: 97.28  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 361 FTNL---QGVAASTNGKILIADS-NNQCVQIFSN-DGQFKSRFGirgrspgQLQRPTGVAVHPSGDIIIADYDNKWVSIF 435
Cdd:cd14952     6 FTGLdgpGGVAVDAAGNVYVADSgNNRVLKLAAGsTTQTVLPFT-------GLYQPQGVAVDAAGTVYVTDFGNNRVLKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 436 SSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNkaccvfifqPNGKIVTRfgsRGNGDRQ----FAGtLDGPHFAAVNS 511
Cdd:cd14952    79 AAGSTTQTVLPFTGLNDPTGVAVDAAGNVYVADT---------GNNRVLKL---AAGSNTQtvlpFTG-LSNPDGVAVDG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 512 NNEIIITDFHNHSVkvfnqegeFMLKFGSNGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRIQVFDgSGSflsyiNTS 588
Cdd:cd14952   146 AGNVYVTDTGNNRV--------LKLAAGSTTQTVLPFtglNSPSGVAVDTAGNVYVTDHGNNRVLKLA-AGS-----TTP 211
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034639127 589 A----DPLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14952   212 TvlpfTGLNGPLGVAVDAAGNVYVADRGND 241
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-584 6.71e-22

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 95.86  E-value: 6.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKsRFGIrgrsPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFS- 436
Cdd:COG4257    56 GGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDpKTGEIT-TFAL----PGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDp 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFgsrgNGDRQFAGtldgPHFAAVNSNNEII 516
Cdd:COG4257   131 ATGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAG----PRGLAVDPDGNLW 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639127 517 ITDFHNHSVKVFN----QEGEFMLKFGSNGegngqfnaPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSY 584
Cdd:COG4257   203 VADTGSGRIGRFDpktgTVTEYPLPGGGAR--------PYGVAVDGDGRVWFAESGANRIVRFDPDTELTEY 266
Filamin pfam00630
Filamin/ABP280 repeat;
200-293 1.66e-21

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 88.89  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 200 ASETVATGEGLRQTIIGQPMSVTITTKDKDGELcktgnaylTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 1034639127 280 LRLYDQHIRGSPFK 293
Cdd:pfam00630  76 VKFNGQHIPGSPFK 89
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
455-617 1.49e-20

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: 92.71  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 455 GVSVDRNGHIIVV-------DNKACCVFIFQPNGKI----VTRFGSRGNGDRQF-AGTLDGPHFAAVNSNNEIIITDFHN 522
Cdd:cd14958    17 GVAVDSLGNGVVFhrggrvwDANSFDANVYVFKGPIeedtILVFDPDGGFLRSWgAGLFYMPHGLTIDPDGNIWVTDVGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 523 HSVKVFNQEGE--FMLKFGSN---GEGNGQFNAPTGVAVDSNGNIIVAD-WGNSRIQVFDGSGSFLSYINTSADPLyG-- 594
Cdd:cd14958    97 HQVFKFDPEGKllPLLTLGERgepGSDQTHFCKPTDVAVAPDGDIFVADgYCNSRIVKFSPDGKLLKSWGEPGSGP-Gqf 175
                         170       180
                  ....*....|....*....|....*...
gi 1034639127 595 --PQGLALTSDGHVVVADSGNH---CFK 617
Cdd:cd14958   176 nlPHSIALDEDGRVYVADRENGriqVFD 203
Bbox2_TRIM2_C-VII cd19824
B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar ...
1-31 5.28e-20

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: 83.18  E-value: 5.28e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKD 31
Cdd:cd19824    12 MEFYCQSCETAMCQECTEGEHAEHPTVPLKD 42
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
537-619 3.69e-19

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 87.72  E-value: 3.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 537 KFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINT---SADPLYGPQGLALTSDGHVVVADSGN 613
Cdd:cd14956     1 SWGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTtgdGPGQFGRPRGLAVDKDGWLYVADYWG 80

                  ....*.
gi 1034639127 614 HCFKVY 619
Cdd:cd14956    81 DRIQVF 86
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
526-614 7.94e-19

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: 87.22  E-value: 7.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 526 KVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADP---LYGPQGLALTS 602
Cdd:cd14954     1 RDYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRdgqFDRPAGVAVNS 80
                          90
                  ....*....|..
gi 1034639127 603 DGHVVVADSGNH 614
Cdd:cd14954    81 RGRIIVADKDNH 92
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
341-576 1.53e-18

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: 86.55  E-value: 1.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 341 NPIEDDLIFRVGTKGR-----NKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIrGRS--PGQLQ---- 409
Cdd:cd14958    50 GPIEEDTILVFDPDGGflrswGAGLFYMPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTL-GERgePGSDQthfc 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 410 RPTGVAVHPSGDIIIAD-YDNKWVSIFSSDGKFKTKIG-SGKLMG----PKGVSVDRNGHIIVVD--NKAccVFIFQPNG 481
Cdd:cd14958   129 KPTDVAVAPDGDIFVADgYCNSRIVKFSPDGKLLKSWGePGSGPGqfnlPHSIALDEDGRVYVADreNGR--IQVFDADG 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 482 KIVTRFGSRGnGDRQFAGTLDG-PHFAAVNSNNEIIiTDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNG 560
Cdd:cd14958   207 KFLTEWTNPE-LGRPYALAIDPdGLLYVVDGPPRLN-RSLPVRGFVIRIGKGLILGRFGPGGKAPGQFQNPHDIAVDSGG 284
                         250
                  ....*....|....*.
gi 1034639127 561 NIIVADWGNSRIQVFD 576
Cdd:cd14958   285 DIYVGELGPNRVQKFV 300
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
491-615 1.82e-18

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: 86.82  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 491 GNGDRQFAG------TLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEfMLKFGSNGE-----GNG---QFNAPTGVAV 556
Cdd:cd14953     6 GSGTAGFSGgggtaaRFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGV-VTTVAGTGTagfadGGGaaaQFNTPSGVAV 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 557 DSNGNIIVADWGNSRI---------QVFDGSGS--FLSYINTSADPLYGPQGLALTSDGHVVVADSGNHC 615
Cdd:cd14953    85 DAAGNLYVADTGNHRIrkitpdgvvSTLAGTGTagFSDDGGATAAQFNYPTGVAVDAAGNLYVADTGNHR 154
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
346-435 2.96e-18

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: 85.29  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14954   196 QFLRFFGSEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVV 275
                          90
                  ....*....|
gi 1034639127 426 DYDNKWVSIF 435
Cdd:cd14954   276 DRGNHRIQVF 285
Bbox2_TRIM2-like cd19759
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and ...
1-31 1.93e-17

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: 75.94  E-value: 1.93e-17
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKD 31
Cdd:cd19759    12 LEFYCESCETAVCRECTAGEHNEHRTVLLKD 42
Bbox2_TRIM3_C-VII cd19825
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
1-31 4.30e-17

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: 75.05  E-value: 4.30e-17
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKD 31
Cdd:cd19825    17 MEFYCESCETAMCRECTEGEHREHVTVPLRD 47
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
342-429 9.66e-16

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 77.71  E-value: 9.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 342 PIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGD 421
Cdd:cd14956   181 DNDGAFLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGT 260

                  ....*...
gi 1034639127 422 IIIADYDN 429
Cdd:cd14956   261 VYVADSNN 268
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
491-619 2.97e-15

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


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 76.09  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 491 GNGDRQFAGTLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEgnGQFNAPTGVAVDSNGNIIVADWGNS 570
Cdd:cd14962     1 VTGEERPKEALTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGP--NRFVSPIGVAIDANGNLYVSDAELG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034639127 571 RIQVFDGSGSFLSYINTSADpLYGPQGLALTSDG-HVVVADSGNHCFKVY 619
Cdd:cd14962    79 KVFVFDRDGKFLRAIGAGAL-FKRPTGIAVDPAGkRLYVVDTLAHKVKVF 127
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
361-572 2.32e-14

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


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 73.01  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 361 FTNL---QGVAASTNGKILIADS-NNQCVQIfsndgqfksrfgIRGRSP------GQLQRPTGVAVHPSGDIIIADYDNK 430
Cdd:cd14952    48 FTGLyqpQGVAVDAAGTVYVTDFgNNRVLKL------------AAGSTTqtvlpfTGLNDPTGVAVDAAGNVYVADTGNN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 431 WVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDnkaccvfifqPNGKIVTRFGSRGNGDRQ--FAGtLDGPHFAA 508
Cdd:cd14952   116 RVLKLAAGSNTQTVLPFTGLSNPDGVAVDGAGNVYVTD----------TGNNRVLKLAAGSTTQTVlpFTG-LNSPSGVA 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639127 509 VNSNNEIIITDFHNHSVkvfnqegefmLKF--GSNGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRI 572
Cdd:cd14952   185 VDTAGNVYVTDHGNNRV----------LKLaaGSTTPTVLPFtglNGPLGVAVDAAGNVYVADRGNDRV 243
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
496-621 2.78e-12

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 67.35  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 496 QFAGTLDGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFgsngeGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 575
Cdd:COG4257    11 PVPAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEY-----PLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRI 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639127 576 DG-SGSFLSYIntSADPLYGPQGLALTSDGHVVVADSGNHcfKVYRY 621
Cdd:COG4257    86 DPkTGEITTFA--LPGGGSNPHGIAFDPDGNLWFTDQGGN--RIGRL 128
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
497-623 8.80e-11

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 62.40  E-value: 8.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 497 FAGTLDGPHFAAVNSNNEIIITDFHNHSVKVFNQE-GEFM--LKFGSNgegngqfnaPTGVAVDSNGN-IIVADWGNSRI 572
Cdd:COG3391    64 AAAVADADGADAGADGRRLYVANSGSGRVSVIDLAtGKVVatIPVGGG---------PRGLAVDPDGGrLYVADSGNGRV 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 573 QVFDG-SGSFLSYINTSAdplyGPQGLALTSDG-HVVVADSGNHcfKVYRYLQ 623
Cdd:COG3391   135 SVIDTaTGKVVATIPVGA----GPHGIAVDPDGkRLYVANSGSN--TVSVIVS 181
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
366-582 9.02e-10

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


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 59.91  E-value: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 366 GVAASTNGKILIADSNNQCVQIFSNDGQFKSRFgirgRSPGQlqRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKI 445
Cdd:COG3386    12 GPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVF----AEPSG--RPNGLAFDPDGRLLVADHGRGLVRFDPADGEVTVLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 446 GSG--KLMGPKGVSVDRNGHIIV----VDNKACCVFIFQPNGKIVTRFG--SRGNGdrqFAGTLDGPHFaavnsnneiII 517
Cdd:COG3386    86 DEYgkPLNRPNDGVVDPDGRLYFtdmgEYLPTGALYRVDPDGSLRVLADglTFPNG---IAFSPDGRTL---------YV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034639127 518 TDFHNHSVKVF--NQEGEFMLK--FGSNGEGNGqfnAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFL 582
Cdd:COG3386   154 ADTGAGRIYRFdlDADGTLGNRrvFADLPDGPG---GPDGLAVDADGNLWVALWGGGGVVRFDPDGELL 219
BBOX smart00336
B-Box-type zinc finger;
1-29 1.30e-09

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 53.88  E-value: 1.30e-09
                           10        20
                   ....*....|....*....|....*....
gi 1034639127    1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:smart00336  14 AEFFCEECGALLCRTCDEAEHRGHTVVLL 42
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
444-621 3.85e-09

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: 57.98  E-value: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 444 KIGSGKLMGPKGVSVDRNGHIIVVDnkaccvfifQPNGKIVtRFGSRGNGDRQFAGTLDGPHFAAVNSNNEIIITDfHNH 523
Cdd:COG3386     1 KLADAGFRLGEGPVWDPDGRLYWVD---------IPGGRIH-RYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVAD-HGR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 524 SVKVFN-QEGEFMLKFGSNGEGNGQFNaptGVAVDSNGNIIVAD----WGNSRIQVFDGSGSflsyINTSADPLYGPQGL 598
Cdd:COG3386    70 GLVRFDpADGEVTVLADEYGKPLNRPN---DGVVDPDGRLYFTDmgeyLPTGALYRVDPDGS----LRVLADGLTFPNGI 142
                         170       180
                  ....*....|....*....|....
gi 1034639127 599 ALTSDG-HVVVADSGNHcfKVYRY 621
Cdd:COG3386   143 AFSPDGrTLYVADTGAG--RIYRF 164
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
543-621 9.47e-09

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


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 56.83  E-value: 9.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 543 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYG-PQGLALTSDGHVVVADSGNHcfKVYRY 621
Cdd:cd14962     6 RPKEALTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGPNRFVsPIGVAIDANGNLYVSDAELG--KVFVF 83
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
345-576 9.59e-09

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 56.24  E-value: 9.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 345 DDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIII 424
Cdd:COG3391     5 SSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 425 ADYDNKWVSIF-SSDGKFKTKIGSGKlmGPKGVSVDRNG-HIIVVDNKACCVFIF-QPNGKIVTRFGsrgngdrqfagTL 501
Cdd:COG3391    85 ANSGSGRVSVIdLATGKVVATIPVGG--GPRGLAVDPDGgRLYVADSGNGRVSVIdTATGKVVATIP-----------VG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 502 DGPHFAAVNS-NNEIIITDFHNHSVKVF-----NQEGEFM--LKFGSNgegngqfnaPTGVAVDSNGNIIV--------A 565
Cdd:COG3391   152 AGPHGIAVDPdGKRLYVANSGSNTVSVIvsvidTATGKVVatIPVGGG---------PVGVAVSPDGRRLYvanrgsntS 222
                         250
                  ....*....|.
gi 1034639127 566 DWGNSRIQVFD 576
Cdd:COG3391   223 NGGSNTVSVID 233
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
347-435 1.12e-08

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: 56.53  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 347 LIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSR----------------------------- 397
Cdd:cd14963   133 LLLEFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKElngspdgksgfvnprgiavdpdgnlyvvd 212
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639127 398 ------------------FGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIF 435
Cdd:cd14963   213 nlshrvyvfdeqgkelftFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
1-37 1.84e-08

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


Pssm-ID: 380854 [Multi-domain]  Cd Length: 48  Bit Score: 50.77  E-value: 1.84e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHK 37
Cdd:cd19796    12 LRLYCDTCSVPICRECTMGEHRGHSFIYLQEAVQDSK 48
zf-B_box pfam00643
B-box zinc finger;
1-29 3.69e-08

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 49.78  E-value: 3.69e-08
                          10        20
                  ....*....|....*....|....*....
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:pfam00643  14 LTLYCNDCQELLCEECSVGEHRGHTVVPL 42
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
548-575 1.45e-07

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 47.78  E-value: 1.45e-07
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 548 FNAPTGVAVDSNGNIIVADWGNSRIQVF 575
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
404-621 3.37e-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: 52.20  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 404 SPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKlMGPKGVSVDRNGHIIVVDNKACcVFIFQP-NGK 482
Cdd:COG3386     3 ADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPS-GRPNGLAFDPDGRLLVADHGRG-LVRFDPaDGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 483 ---IVTRFGSRGNGdrqfagtldgPHFAAVNSNNEIIITDFHNH----SVKVFNQEGEFMLKFGSngegngqFNAPTGVA 555
Cdd:COG3386    81 vtvLADEYGKPLNR----------PNDGVVDPDGRLYFTDMGEYlptgALYRVDPDGSLRVLADG-------LTFPNGIA 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 556 VDSNGNI-IVADWGNSRIQVFD--GSGSfLS----YINTSADPlYGPQGLALTSDGHVVVADSGNHCfkVYRY 621
Cdd:COG3386   144 FSPDGRTlYVADTGAGRIYRFDldADGT-LGnrrvFADLPDGP-GGPDGLAVDADGNLWVALWGGGG--VVRF 212
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
511-621 2.42e-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: 50.02  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 511 SNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVD-SNGNIIVADWGNSRIQVFD-GSGSFLSYINTS 588
Cdd:pfam17170  52 VDDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDkSNNSIYILDFMQNKILTYDlDGYSFIGEINLD 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639127 589 ADP-----------LYGPQGLA--LTSDGHVVVADS-GNHCFKVYRY 621
Cdd:pfam17170 132 LLPsdccqldkgklAFDSSGFDdgKRSGFYLVITDElGNIISGFFPA 178
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
592-619 3.98e-06

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 43.54  E-value: 3.98e-06
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 592 LYGPQGLALTSDGHVVVADSGNHCFKVY 619
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
1-29 8.92e-06

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: 42.78  E-value: 8.92e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034639127   1 MEFYCQSCETAMCREC-TEGEHAEHPTVPL 29
Cdd:cd19756    10 LKLFCETCQELVCVLClLSGEHRGHKVVPL 39
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
352-576 1.38e-05

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: 47.57  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 352 GTKGRNKGEFT-----NLQGVAASTNGKILIADSNNQCV-QI-FSN--------DGQfKSRFGIRGRSPGQ--LQRPTGV 414
Cdd:cd14951     4 GERGLKDGSFAeasfnEPQGLALLPGNILYVADTENHALrKIdLETgtvttlagTGE-QGRDGEGGGPGREqpLSSPWDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 415 AVHPSGDII-IA----------DYDNKWVSIFSsdgkfktkiGSGK---LMG----------PKGVSVDRNGHIIV---- 466
Cdd:cd14951    83 AWGPEDDILyIAmagthqiwayDLDTGTCRVFA---------GSGNegnRNGpypheawfaqPSGLSLAGWGELFVadse 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 467 ------VDNKAccvfifqpnGKIVTRFGSRGNGDRQFA-GTLDGPHFAA---------VNSNNEIIITDFHNHSVKVFN- 529
Cdd:cd14951   154 ssairaVSLKD---------GGVKTLVGGTRVGTGLFDfGDRDGPGAEAllqhplgvaALPDGSVYVADTYNHKIKRVDp 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034639127 530 --QEGEFMLKFGSNGEGN--GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 576
Cdd:cd14951   225 atGEVSTLAGTGKAGYKDleAQFSEPSGLVVDGDGRLYVADTNNHRIRRLD 275
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
361-576 1.39e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 48.31  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  361 FTNLQGVAASTNGKIL-IADSNN----------QCVQIFSNDGQFKSRFgiRGRSPGQLQ---RPTGVAVHPSGDII--- 423
Cdd:PLN02919   623 FNRPQGLAYNAKKNLLyVADTENhalreidfvnETVRTLAGNGTKGSDY--QGGKKGTSQvlnSPWDVCFEPVNEKVyia 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  424 ------IADYD--NKWVSIFSSDGKFKTKIGSG----KLMGPKGVSVDRN-GHIIVVDNKACCVFIFQpngkiVTRFGSR 490
Cdd:PLN02919   701 magqhqIWEYNisDGVTRVFSGDGYERNLNGSSgtstSFAQPSGISLSPDlKELYIADSESSSIRALD-----LKTGGSR 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  491 --GNGDRQFAGTL------DGP-------HFAAV--NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGN-------- 545
Cdd:PLN02919   776 llAGGDPTFSDNLfkfgdhDGVgsevllqHPLGVlcAKDGQIYVADSYNHKIKKLDPATKRVTTLAGTGKAGfkdgkalk 855
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034639127  546 GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 576
Cdd:PLN02919   856 AQLSEPAGLALGENGRLFVADTNNSLIRYLD 886
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
501-528 1.39e-05

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 42.00  E-value: 1.39e-05
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 501 LDGPHFAAVNSNNEIIITDFHNHSVKVF 528
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
551-614 2.28e-05

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: 46.80  E-value: 2.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639127 551 PTGVAVDSNGNIIVADWGNSRIQVFD----------GSGSFLSYINTSAdpLYGPQGLALTSDGHVVVADSGNH 614
Cdd:cd14951   198 PLGVAALPDGSVYVADTYNHKIKRVDpatgevstlaGTGKAGYKDLEAQ--FSEPSGLVVDGDGRLYVADTNNH 269
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
356-620 2.82e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 46.17  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 356 RNKGEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRFGirgrspGQLQRPTGVAVHPSGDIIIADYDNKWVSI 434
Cdd:cd00200    46 TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDlETGECVRTLT------GHTSYVSSVAFSPDGRILSSSSRDKTIKV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 435 FS-SDGKFKTKIgSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP-NGKIVTrfgsrgngdrqfagTLDGpHFAAVNS- 511
Cdd:cd00200   120 WDvETGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLrTGKCVA--------------TLTG-HTGEVNSv 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 512 ----NNEIIITDFHNHSVKVFNQEGEFMLKfgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDG-SGSFLSyin 586
Cdd:cd00200   184 afspDGEKLLSSSSDGTIKLWDLSTGKCLG-----TLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLrTGECVQ--- 255
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034639127 587 tsadPLYGPQG----LALTSDGHVVVADSGNHCFKVYR 620
Cdd:cd00200   256 ----TLSGHTNsvtsLAWSPDGKRLASGSADGTIRIWD 289
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
34-190 2.91e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.12  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  34 EQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHstfdELQKTLNVRksvllmELEVNyGLKHKV-- 111
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR----DLKDMLDVK------ERKIN-VLQKKIen 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 112 LQSQL---DTLLQG-QESIKSC---SNFTAQALnhGTETEVLLVKKQMSEKLNEladqdfplhPRENDQLDFIVETEGLK 184
Cdd:pfam10174 406 LQEQLrdkDKQLAGlKERVKSLqtdSSNTDTAL--TTLEEALSEKERIIERLKE---------QREREDRERLEELESLK 474

                  ....*.
gi 1034639127 185 KSIHNL 190
Cdd:pfam10174 475 KENKDL 480
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
461-593 3.68e-05

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 46.17  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 461 NGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGTLDgphFAAVNSNNEIIITDFHNHSVKVFNQEG-EFM---- 535
Cdd:pfam17170  53 DDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQIND---FIIDKSNNSIYILDFMQNKILTYDLDGySFIgein 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639127 536 ---------------LKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRiqvfdgsgsFLSYINTSADPLY 593
Cdd:pfam17170 130 ldllpsdccqldkgkLAFDSSGFDDGKRSGFYLVITDELGNIISGFFPAEF---------TLGILFNSSVPFY 193
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
1-37 4.98e-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: 4.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHK 37
Cdd:cd19769    10 LELFCRTDQMCICELCAKEEHRGHDVVTVEEEREKKE 46
Bbox2_TRIM56_C-V cd19789
B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar ...
1-33 6.39e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380847  Cd Length: 47  Bit Score: 40.60  E-value: 6.39e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034639127   1 MEFYCQSCETAMCRECTEGEHAE--HPTVPLKDVV 33
Cdd:cd19789    13 LLLYCTPCEAAVCRECRLRPHLSltHRCLPLAEAA 47
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
408-435 7.83e-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: 39.69  E-value: 7.83e-05
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 408 LQRPTGVAVHPSGDIIIADYDNKWVSIF 435
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
411-620 2.41e-04

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 43.74  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 411 PTGVAVHPSGDIIIA--DYDNKWVSIFS---SDGKFkTKIGSGKLMG--PKGVSVDRNGHIIVVDN---KACCVFIFQPN 480
Cdd:COG2706    47 PSFLALSPDGRFLYAvnEVDDGGVSAFRidpADGTL-TLLNTVSSGGasPCHLSVDPDGRFLFVANyggGSVSVFPIDAD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 481 GKI------VTRFGSRGNGDRQfagTLDGPHFAAVN-SNNEIIITDFHNHSVKVFN---------QEGEFMLKFGS---- 540
Cdd:COG2706   126 GSLgepvqvIQHEGSGPNPERQ---EGPHAHSVVFDpDGRFLYVPDLGTDRIYVYRldpatgklpEPPEVSLPPGSgprh 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 541 -----NG-------------------EGNGQF----------------NAPTGVAVDSNGN-IIVADWGNSRIQVF---- 575
Cdd:COG2706   203 lafhpNGrfayvineldstvsvyaydAATGTLtliqtvstlpedftgeNWAADIHISPDGRfLYVSNRGHNSIAVFaida 282
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639127 576 -DGSGSFLSYINTSADplyGPQGLALTSDG-HVVVADSGNHCFKVYR 620
Cdd:COG2706   283 dGGKLTLVGHVPTGGK---WPRDFAIDPDGrFLLVANQKSDNITVFR 326
Bbox2_TRIM45_C-X cd19785
B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar ...
3-32 2.51e-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: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034639127   3 FYCQSCETAMCRECTEGEHAEHPTVPLKDV 32
Cdd:cd19785    14 LFCETCDKPVCRDCVLVEHRGHQCDFTSDV 43
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
361-388 3.06e-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: 38.15  E-value: 3.06e-04
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 361 FTNLQGVAASTNGKILIADSNNQCVQIF 388
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
WD40 COG2319
WD40 repeat [General function prediction only];
366-620 3.62e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.36  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 366 GVAASTNGKILIADSNNQCVQIFS-NDGQFKSRFgirgrsPGQLQRPTGVAVHPSGDIII-ADYDNKwVSIFSSDGKFKT 443
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTL------TGHTGAVRSVAFSPDGKLLAsGSADGT-VRLWDLATGKLL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 444 KIGSGKLMGPKGVSVDRNGHIIVV---DNKaccVFIFQPN-GKIVTRFGSRGNGDRQFAGTLDGPHFAAVNSNNeiiitd 519
Cdd:COG2319   240 RTLTGHSGSVRSVAFSPDGRLLASgsaDGT---VRLWDLAtGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG------ 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 520 fhnhSVKVFN-QEGEFMLKFgsngegNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLsyINTSADPLYGPQGL 598
Cdd:COG2319   311 ----TVRLWDlATGKLLRTL------TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL--LRTLTGHTGAVTSV 378
                         250       260
                  ....*....|....*....|..
gi 1034639127 599 ALTSDGHVVVADSGNHCFKVYR 620
Cdd:COG2319   379 AFSPDGRTLASGSADGTVRLWD 400
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
344-388 3.63e-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: 42.92  E-value: 3.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034639127 344 EDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIF 388
Cdd:cd14954   241 DGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
371-439 4.72e-04

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


Pssm-ID: 407298 [Multi-domain]  Cd Length: 321  Bit Score: 42.70  E-value: 4.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 371 TNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDII-IADYDNKWVSIFSSDG 439
Cdd:pfam17170  52 VDDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDKSNNSIyILDFMQNKILTYDLDG 121
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
548-609 5.20e-04

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


Pssm-ID: 467996 [Multi-domain]  Cd Length: 330  Bit Score: 42.65  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639127 548 FNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSfLSYI------NTSADPLYGPQGLALTSDGHVVVA 609
Cdd:NF033206  249 FTGLTDLAFDPDGNLYVLELAGGGLLKGDPTGS-LIRIapdgtrTTLLDGLELPTGLAVGPDGTLYVT 315
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
533-622 6.39e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 42.92  E-value: 6.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  533 EFMLKFGSN-GEG-NGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTS-----------ADPLYGPQGLA 599
Cdd:PLN02919   786 DNLFKFGDHdGVGsEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPATKRVTTLAGTgkagfkdgkalKAQLSEPAGLA 865
                           90       100
                   ....*....|....*....|...
gi 1034639127  600 LTSDGHVVVADSGNhcfKVYRYL 622
Cdd:PLN02919   866 LGENGRLFVADTNN---SLIRYL 885
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
512-621 9.23e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 42.53  E-value: 9.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127  512 NNEIIITDFHNHSVKVFNQEGEFMLKFGSNGE--------GNGQFNAPTGVAVDSNGNII-VA----------DWGNSRI 572
Cdd:PLN02919   579 NNRLFISDSNHNRIVVTDLDGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKNLLyVAdtenhalreiDFVNETV 658
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034639127  573 QVFDGSGS----FLSYINTSADPLYGPQGLALTS-DGHVVVADSGNHcfKVYRY 621
Cdd:PLN02919   659 RTLAGNGTkgsdYQGGKKGTSQVLNSPWDVCFEPvNEKVYIAMAGQH--QIWEY 710
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
550-579 1.13e-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: 41.09  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034639127 550 APTGVAVDSNGNIIVADWGNSRIQVFDGSG 579
Cdd:pfam08450 185 RPDGMAVDAEGNVWVARWGGGKVVRFDPDG 214
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
343-487 1.99e-03

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: 40.26  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 343 IEDDLIFRVGTKGRNKGEFTNLQ----GVAASTNGKILIADSNNQCVQIFSNDGQFK---SRFGIRGRSP---------- 405
Cdd:COG3386    26 IPGGRIHRYDPDGGAVEVFAEPSgrpnGLAFDPDGRLLVADHGRGLVRFDPADGEVTvlaDEYGKPLNRPndgvvdpdgr 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639127 406 ---------------------GQLQR-------PTGVAVHPSGDI-IIADYDNKWVSIF--SSDGK-------FKTKIGS 447
Cdd:COG3386   106 lyftdmgeylptgalyrvdpdGSLRVladgltfPNGIAFSPDGRTlYVADTGAGRIYRFdlDADGTlgnrrvfADLPDGP 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034639127 448 GklmGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRF 487
Cdd:COG3386   186 G---GPDGLAVDADGNLWVALWGGGGVVRFDPDGELLGRI 222
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
450-477 2.06e-03

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


Pssm-ID: 396153 [Multi-domain]  Cd Length: 28  Bit Score: 35.84  E-value: 2.06e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034639127 450 LMGPKGVSVDRNGHIIVVDNKACCVFIF 477
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
595-614 9.38e-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: 38.71  E-value: 9.38e-03
                          10        20
                  ....*....|....*....|
gi 1034639127 595 PQGLALTSDGHVVVADSGNH 614
Cdd:cd14951    21 PQGLALLPGNILYVADTENH 40
Bbox2_GefO-like cd20207
B-box-type 2 zinc finger found in Ras guanine nucleotide exchange factor O (GefO) and similar ...
4-29 9.90e-03

B-box-type 2 zinc finger found in Ras guanine nucleotide exchange factor O (GefO) and similar proteins; Ras guanine-nucleotide exchange factors (RasGEFs) activate Ras by catalyzing the replacement of GDP with GTP, and thus lie near the top of many signaling pathways. They are important for signaling in development and chemotaxis in many organisms. Ras guanine nucleotide exchange factor O (GefO), also known as RasGEF domain-containing protein O, is faintly expressed during development of Dictyostelium discoideum. It contains a C3HC4-type RING finger, a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs), a REM (Ras exchanger motif) domain, and a # RasGEF domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380908  Cd Length: 40  Bit Score: 34.43  E-value: 9.90e-03
                          10        20
                  ....*....|....*....|....*.
gi 1034639127   4 YCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:cd20207    14 FCKDCSAPVCENCVLTTHAGHNVEPI 39
 
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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