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Conserved domains on  [gi|1189131358|ref|NP_001337986|]
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tripartite motif-containing protein 2 isoform 9 [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; ...
346-619 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: 583.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAV 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 506 NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSA 585
Cdd:cd14960   161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1189131358 586 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 619
Cdd:cd14960   241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 8.62e-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: 8.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1189131358  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 1.92e-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: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1189131358  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 5.25e-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: 5.25e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1189131358   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; ...
346-619 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: 583.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAV 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 506 NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSA 585
Cdd:cd14960   161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1189131358 586 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 619
Cdd:cd14960   241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 8.62e-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: 8.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1189131358  116 LDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQ 162
Cdd:smart00502  81 LESLTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNLLKQ 127
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-617 7.89e-30

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 118.58  E-value: 7.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRfgirgrSPGQLQRPTGVAVHPSGDIIIADY-DNKWVSIFS 436
Cdd:COG4257    14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFTEY------PLGGGSGPHGIAVDPDGNLWFTDNgNNRIGRIDP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGdrqfAGPHFAAVNSNNEIIITDF 516
Cdd:COG4257    88 KTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPLPTGG----AGPYGIAVDPDGNLWVTDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 517 HNHSVKVFNQEGEFMLKFgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-GSGSFLSYinTSADPLYGPQGLA 595
Cdd:COG4257   164 GANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGARPYGVA 237
                         250       260
                  ....*....|....*....|..
gi 1189131358 596 LTSDGHVVVADSGNHcfKVYRY 617
Cdd:COG4257   238 VDGDGRVWFAESGAN--RIVRF 257
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
36-157 1.04e-26

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: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1189131358 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 1.92e-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: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1189131358  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 1189131358 200 ASETVATGEGLRQTIIGQPMSVTITTKDKDGELcktgnaylTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 1189131358 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 5.25e-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: 5.25e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1189131358   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 1189131358    1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:smart00336  14 AEFFCEECGALLCRTCDEAEHRGHTVVLL 42
zf-B_box pfam00643
B-box zinc finger;
1-29 3.97e-08

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 49.39  E-value: 3.97e-08
                          10        20
                  ....*....|....*....|....*....
gi 1189131358   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 ...
544-571 1.44e-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: 1.44e-07
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 544 FNAPTGVAVDSNGNIIVADWGNSRIQVF 571
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
372-572 2.10e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 47.92  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  372 NGKILIA----------DSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQrPTGVAVHPSGD-IIIADYDNKwvSIFSSDgk 440
Cdd:PLN02919   694 NEKVYIAmagqhqiweyNISDGVTRVFSGDGYERNLNGSSGTSTSFAQ-PSGISLSPDLKeLYIADSESS--SIRALD-- 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  441 FKTKiGSGKLMGpkgvsvdrnGHIIVVDNkaccvfIFQpngkivtrFGSR-GNGDR-QFAGPHFAAVNSNNEIIITDFHN 518
Cdd:PLN02919   769 LKTG-GSRLLAG---------GDPTFSDN------LFK--------FGDHdGVGSEvLLQHPLGVLCAKDGQIYVADSYN 824
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131358  519 HSVKVFNQEGEFMLKFGSNGEGN--------GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 572
Cdd:PLN02919   825 HKIKKLDPATKRVTTLAGTGKAGfkdgkalkAQLSEPAGLALGENGRLFVADTNNSLIRYLD 886
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
34-190 2.88e-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: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  34 EQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHstfdELQKTLNVRksvllmELEVNyGLKHKV-- 111
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR----DLKDMLDVK------ERKIN-VLQKKIen 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 112 LQSQL---DTLLQG-QESIKSC---SNFTAQALnhGTETEVLLVKKQMSEKLNEladqdfplhPRENDQLDFIVETEGLK 184
Cdd:pfam10174 406 LQEQLrdkDKQLAGlKERVKSLqtdSSNTDTAL--TTLEEALSEKERIIERLKE---------QREREDRERLEELESLK 474

                  ....*.
gi 1189131358 185 KSIHNL 190
Cdd:pfam10174 475 KENKDL 480
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
544-605 4.89e-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: 4.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131358 544 FNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSfLSYI------NTSADPLYGPQGLALTSDGHVVVA 605
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; ...
346-619 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: 583.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14960     1 DLIFRIGTKGRNKGEFTNLQGVAASSSGRLVIADSNNQCVQVFSNDGQFKLRFGVRGRSPGQLQRPTGVAVTLNGDIIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 426 DYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAV 505
Cdd:cd14960    81 DYDNKWVSIFSPDGKFKSKIGAGKLMGPKGVAVDRNGHIIVVDNKACCVFIFQPNGKLVTRFGSRGNGDRQFAGPHFAAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 506 NSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSA 585
Cdd:cd14960   161 NNNNEIIVTDFHNHSVKVFNAEGEFLFKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSA 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1189131358 586 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 619
Cdd:cd14960   241 DPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ 274
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
355-615 1.16e-96

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: 296.92  E-value: 1.16e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 355 GRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSI 434
Cdd:cd05819     1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSFGSFGSGDGQFNEPAGVAVDSDGNLYVADTGNHRIQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 435 FSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNN 509
Cdd:cd05819    81 FDPDGNFLASFGGsgdgdGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGSGGSGPGQFNGPTGVAVDSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 510 EIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS---YINTSAD 586
Cdd:cd05819   161 NIYVADTGNHRIQVFDPDGNFLTTFGSTGTGPGQFNYPTGIAVDSDGNIYVADSGNNRVQVFDPDGAGFGgngNFLGSDG 240
                         250       260
                  ....*....|....*....|....*....
gi 1189131358 587 PLYGPQGLALTSDGHVVVADSGNHCFKVY 615
Cdd:cd05819   241 QFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
347-615 4.09e-91

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: 282.90  E-value: 4.09e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 347 LIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIAD 426
Cdd:cd14954     9 PLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRDGQFDRPAGVAVNSRGRIIVAD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 427 YDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPH 501
Cdd:cd14954    89 KDNHRIQVFDLNGRFLLKFGErgtknGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPGQLDSPR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 502 FAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI 581
Cdd:cd14954   169 GVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSF 248
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1189131358 582 NT---SADPLYGPQGLALTSDGHVVVADSGNHCFKVY 615
Cdd:cd14954   249 GTegnGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
352-611 1.73e-80

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: 255.19  E-value: 1.73e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14955     6 GSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVADTGNHR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVN 506
Cdd:cd14955    86 IQKFDSTGTFLTKWGSsgsgdGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQFNSPTGIAVD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 507 SNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS---YINT 583
Cdd:cd14955   166 SAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVDSAGNVYVADTGNNRIQKFDSSGTFITkwgSEGS 245
                         250       260
                  ....*....|....*....|....*...
gi 1189131358 584 SADPLYGPQGLALTSDGHVVVADSGNHC 611
Cdd:cd14955   246 GDGQFNSPSGIAVDSAGNVYVADSGNNR 273
NHL_like_2 cd14957
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
345-616 8.46e-72

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: 232.54  E-value: 8.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 345 DDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIII 424
Cdd:cd14957     1 ASFSYAFGSNGSGNGQFNTPRGIAVDSAGNIYVADTGNNRIQVFTSSGVYSYSIGSGGTGSGQFNSPYGIAVDSNGNIYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 425 ADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAG 499
Cdd:cd14957    81 ADTDNNRIQVFNSSGVYQYSIGTggsgdGQFNGPYGIAVDSNGNIYVADTGNHRIQVFTSSGTFSYSIGSGGTGPGQFNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 500 PHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS 579
Cdd:cd14957   161 PQGIAVDSDGNIYVADTGNHRIQVFTSSGTFQYTFGSSGSGPGQFSDPYGIAVDSDGNIYVADTGNHRIQVFTSSGAYQY 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1189131358 580 YINTSADPLYG---PQGLALTSDGHVVVADSGNHCFKVYR 616
Cdd:cd14957   241 SIGTSGSGNGQfnyPYGIAVDNDGKIYVADSNNNRIQVFN 280
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
352-610 6.45e-69

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: 224.85  E-value: 6.45e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14956     3 GGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVN 506
Cdd:cd14956    83 IQVFTLTGELQTIGGSsgsgpGQFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIEPGSFNYPRGVAVD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 507 SNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSAD 586
Cdd:cd14956   163 PDGTLYVADTYNDRIQVFDNDGAFLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGT 242
                         250       260
                  ....*....|....*....|....*..
gi 1189131358 587 ---PLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14956   243 gpgQFKNPWGVVVDADGTVYVADSNNN 269
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
388-610 9.81e-64

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


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 211.64  E-value: 9.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 388 FSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNG 462
Cdd:cd14954     3 YRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSygsrdGQFDRPAGVAVNSRG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 463 HIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNG 542
Cdd:cd14954    83 RIIVADKDNHRIQVFDLNGRFLLKFGERGTKNGQFNYPWGVAVDSEGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189131358 543 QFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSAD---PLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14954   163 QLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSgngQFKRPRGVAVDDEGNIIVADSGNH 233
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
352-616 6.27e-60

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: 200.97  E-value: 6.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14961     1 GSFGGWPGTLNNPTGVAVTPTGRVVVADDGNKRIQVFDSDGNCLQQFGPKGDAGQDIRYPLDVAVTPDGHIVVTDAGDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 432 VSIFSSDGKFKTKIGSGKLMgPKGVSVDRNGHIIVVDNKACCVFIFQPNGKiVTRFGSRGNGDRQFAGPHFAAVNSNNEI 511
Cdd:cd14961    81 VKVFSFDGRLKLFVRKSFSL-PWGVAVNPSGEILVTDSEAGKLFVLTVDFK-LGILKKGQKLCSQLCRPRFVAVSRLGAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 512 IITD--------FHNHSVKVFNQEGEF---MLKFGsNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSY 580
Cdd:cd14961   159 AVTEhlfangtrSSSTRVKVFSSGGQLlgqIDSFG-LNLVFPSLICASGVAFDSEGNVIVADTGSGAILCLGKPEGFPIL 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1189131358 581 INTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYR 616
Cdd:cd14961   238 KPIVTQGLSRPVGLAVTPDGSLVVLDSGNHCVKIYK 273
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
352-572 7.90e-59

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: 198.57  E-value: 7.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14955    53 GSSGSGDGQFYSPTGIAVDSDGNVYVADTGNHRIQKFDSTGTFLTKWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSGNNR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVN 506
Cdd:cd14955   133 IQKFDSSGTFITKWGSfgsgdGQFNSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVD 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189131358 507 SNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 572
Cdd:cd14955   213 SAGNVYVADTGNNRIQKFDSSGTFITKWGSEGSGDGQFNSPSGIAVDSAGNVYVADSGNNRIQKFA 278
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
394-610 1.92e-57

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: 194.72  E-value: 1.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 394 FKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVD 468
Cdd:cd14955     1 FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSsgsgdGQFYSPTGIAVDSDGNVYVAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 469 NKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPT 548
Cdd:cd14955    81 TGNHRIQKFDSTGTFLTKWGSSGSGDGQFNSPSGIAVDSAGNVYVTDSGNNRIQKFDSSGTFITKWGSFGSGDGQFNSPT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189131358 549 GVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTS---ADPLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14955   161 GIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEgsgDGQFNAPYGIAVDSAGNVYVADTGNN 225
NHL_brat_like cd14959
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ...
346-618 6.08e-54

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: 185.17  E-value: 6.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 346 DLIFR--VGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAV-HPSGDI 422
Cdd:cd14959     4 KMIIHckFGESGSGEGQFNSPSGFCLGEDEDILVADTNNHRIQVFDKEGEFKFQFGIPGKRDGQLWYPNKVAVcRVTGRY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 423 IIADYDNK--WVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSrgngDRQFAGP 500
Cdd:cd14959    84 VVTDRGNPrhRMQIFTKRGQFVRKFGARYLQHVRGLTVDAAGHIIVVESKVMRVFIFDESGNVLKWFDC----SKYLEEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 501 HFAAVNsNNEIIITDFHNHSVKVFNQEGEFMLKFGsngeGNGQFNAPTGVAVDSNGNIIVADWGNSR--IQVFDGSGSFL 578
Cdd:cd14959   160 SDVAVN-DNEIYICDNKGHCVVVFNYDGQFLRRIG----GEGITNYPIGVDISSAGDVLVADNHGNHfhVTVFTRDGQLI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1189131358 579 SYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYL 618
Cdd:cd14959   235 SEFECPRVKHSRCCGLALTSEGSIVTLSKHNHHVLVFNTL 274
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
366-615 1.78e-53

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: 183.65  E-value: 1.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 366 GVAAStNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKI 445
Cdd:cd14963    14 GVAVS-DGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKYF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 446 GSGK----LMGPKGVSVDRnGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSV 521
Cdd:cd14963    93 PEKKdrvkLISPAGLAIDD-GKLYVSDVKKHKVIVFDLEGKLLLEFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 522 KVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSAD---PLYGPQGLALTS 598
Cdd:cd14963   172 QVFDKNGKFIKELNGSPDGKSGFVNPRGIAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKddgQFNLPNGLFIDD 251
                         250
                  ....*....|....*..
gi 1189131358 599 DGHVVVADSGNHCFKVY 615
Cdd:cd14963   252 DGRLYVTDRENNRVAVY 268
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
365-618 3.50e-53

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: 183.17  E-value: 3.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 365 QGVAASTNGKILIADSNNQCVQIFsnDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTK 444
Cdd:cd14962    15 YGVAADGRGRIYVADTGRGAVFVF--DLPNGKVFVIGNAGPNRFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 445 IGSGKLMG-PKGVSVD-RNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVK 522
Cdd:cd14962    93 IGAGALFKrPTGIAVDpAGKRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNLPTDLAVDRDGNLYVTDTMNFRVQ 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 523 VFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYI-NTSADP--LYGPQGLALTSD 599
Cdd:cd14962   173 IFDADGKFLRSFGERGDGPGSFARPKGIAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVgGPGSGPgeFYLPSGIAIDKD 252
                         250
                  ....*....|....*....
gi 1189131358 600 GHVVVADSGNHCFKVYRYL 618
Cdd:cd14962   253 DRIYVVDQFNRRIQVFQYL 271
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
343-571 3.39e-50

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: 174.81  E-value: 3.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 343 IEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDI 422
Cdd:cd05819    83 PDGNFLASFGGSGDGDGEFNGPRGIAVDSSGNIYVADTGNHRIQKFDPDGEFLTTFGSGGSGPGQFNGPTGVAVDSDGNI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 423 IIADYDNkwvsifssdgkfktkigsgklmgpkgvsvdrnghiivvdnkaCCVFIFQPNGKIVTRFGSRGNGDRQFAGPHF 502
Cdd:cd05819   163 YVADTGN------------------------------------------HRIQVFDPDGNFLTTFGSTGTGPGQFNYPTG 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189131358 503 AAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 571
Cdd:cd05819   201 IAVDSDGNIYVADSGNNRVQVFDPDGAGFGGNGNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
348-571 9.01e-47

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: 165.54  E-value: 9.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 348 IFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGiRGRSPGQLQRPTGVAVHpSGDIIIADY 427
Cdd:cd14963    42 KKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDGKFLKYFP-EKKDRVKLISPAGLAID-DGKLYVSDV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 428 DNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHF 502
Cdd:cd14963   120 KKHKVIVFDLEGKLLLEFGKpgsepGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKELNGSPDGKSGFVNPRG 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189131358 503 AAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 571
Cdd:cd14963   200 IAVDPDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKDDGQFNLPNGLFIDDDGRLYVTDRENNRVAVY 268
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
350-571 1.58e-43

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: 156.98  E-value: 1.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 350 RVGTKGRNKGE-FTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGirgrSPGQLQRPTGVAVHPSGD-IIIADY 427
Cdd:cd14962    44 KVFVIGNAGPNrFVSPIGVAIDANGNLYVSDAELGKVFVFDRDGKFLRAIG----AGALFKRPTGIAVDPAGKrLYVVDT 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 428 DNKWVSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHF 502
Cdd:cd14962   120 LAHKVKVFDLDGRLLFDIGKrgsgpGEFNLPTDLAVDRDGNLYVTDTMNFRVQIFDADGKFLRSFGERGDGPGSFARPKG 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189131358 503 AAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVF 571
Cdd:cd14962   200 IAVDSEGNIYVVDAAFDNVQIFNPEGELLLTVGGPGSGPGEFYLPSGIAIDKDDRIYVVDQFNRRIQVF 268
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
361-610 5.47e-38

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: 143.05  E-value: 5.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 361 FTNLQGVAASTNGKILIADSNNQCVQIFSNDGQfKSRF---GIRGRSPG-----QLQRPTGVAVHPSGDIIIADYDNKWV 432
Cdd:cd14953    22 FNSPSGVAVDAAGNLYVADRGNHRIRKITPDGV-VTTVagtGTAGFADGggaaaQFNTPSGVAVDAAGNLYVADTGNHRI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 433 SIFSSDGKFKTKIGSG-------------KLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVT-----RFGSRGNG- 493
Cdd:cd14953   101 RKITPDGVVSTLAGTGtagfsddggataaQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVTTvagtgGAGYAGDGp 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 494 --DRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEG--------NGQFNAPTGVAVDSNGNIIVADW 563
Cdd:cd14953   181 atAAQFNNPTGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGTAGfsgdggatAAQLNNPTGVAVDAAGNLYVADS 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131358 564 GNSRI----------QVFDGSGSFLSYINTSAD-PLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14953   261 GNHRIrkitpagvvtTVAGGGAGFSGDGGPATSaQFNNPTGVAVDAAGNLYVADTGNN 318
NHL_like_4 cd14955
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ...
483-611 7.54e-38

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: 141.56  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 483 IVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVAD 562
Cdd:cd14955     1 FVTQWGSYGSGDGQFNSPSGIAVDSAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSGDGQFYSPTGIAVDSDGNVYVAD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1189131358 563 WGNSRIQVFDGSGSFLSYINTSAD---PLYGPQGLALTSDGHVVVADSGNHC 611
Cdd:cd14955    81 TGNHRIQKFDSTGTFLTKWGSSGSgdgQFNSPSGIAVDSAGNVYVTDSGNNR 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
36-162 8.62e-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: 8.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358   36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1189131358  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 ...
405-609 1.57e-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: 130.08  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 405 PGQLQRPTGVAVHPSGDIII-ADYDNKWVS--------------------IFSSDGKFKTKIGSGKLMGPKGVSVDRNGH 463
Cdd:cd14958     9 SLKLGQVSGVAVDSLGNGVVfHRGGRVWDAnsfdanvyvfkgpieedtilVFDPDGGFLRSWGAGLFYMPHGLTIDPDGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 464 IIVVDNKACCVFIFQPNGKIVTR--FGSR---GNGDRQFAGPHFAAVNSNNEIIITDFH-NHSVKVFNQEGEFMLKFGSN 537
Cdd:cd14958    89 IWVTDVGLHQVFKFDPEGKLLPLltLGERgepGSDQTHFCKPTDVAVAPDGDIFVADGYcNSRIVKFSPDGKLLKSWGEP 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189131358 538 GEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLS-YINTSADPLYgpqGLALTSDGHVVVADSGN 609
Cdd:cd14958   169 GSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLTeWTNPELGRPY---ALAIDPDGLLYVVDGPP 238
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-617 7.89e-30

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 118.58  E-value: 7.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRfgirgrSPGQLQRPTGVAVHPSGDIIIADY-DNKWVSIFS 436
Cdd:COG4257    14 APGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEFTEY------PLGGGSGPHGIAVDPDGNLWFTDNgNNRIGRIDP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGdrqfAGPHFAAVNSNNEIIITDF 516
Cdd:COG4257    88 KTGEITTFALPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPLPTGG----AGPYGIAVDPDGNLWVTDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 517 HNHSVKVFNQEGEFMLKFgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFD-GSGSFLSYinTSADPLYGPQGLA 595
Cdd:COG4257   164 GANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDpKTGTVTEY--PLPGGGARPYGVA 237
                         250       260
                  ....*....|....*....|..
gi 1189131358 596 LTSDGHVVVADSGNHcfKVYRY 617
Cdd:COG4257   238 VDGDGRVWFAESGAN--RIVRF 257
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
407-611 3.40e-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: 118.40  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 407 QLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSG------------KLMGPKGVSVDRNGHIIVVDNKACCV 474
Cdd:cd14953    21 RFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGVVTTVAGTGtagfadgggaaaQFNTPSGVAVDAAGNLYVADTGNHRI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 475 FIFQPNGKIVTRFGSRGNGDR--------QFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFM-----LKFGSNGEGN 541
Cdd:cd14953   101 RKITPDGVVSTLAGTGTAGFSddggataaQFNYPTGVAVDAAGNLYVADTGNHRIRKITPDGVVTtvagtGGAGYAGDGP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 542 G---QFNAPTGVAVDSNGNIIVADWGNSRIQVFD---------GSGSFLS---YINTSAdPLYGPQGLALTSDGHVVVAD 606
Cdd:cd14953   181 AtaaQFNNPTGVAVDAAGNLYVADRGNHRIRKITpdgvvttvaGTGTAGFsgdGGATAA-QLNNPTGVAVDAAGNLYVAD 259

                  ....*
gi 1189131358 607 SGNHC 611
Cdd:cd14953   260 SGNHR 264
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
352-568 8.86e-28

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: 114.16  E-value: 8.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKG-----EFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFkSRF---GIRGRSPG------QLQRPTGVAVH 417
Cdd:cd14953    62 GTAGFADGggaaaQFNTPSGVAVDAAGNLYVADTGNHRIRKITPDGVV-STLagtGTAGFSDDggataaQFNYPTGVAVD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 418 PSGDIIIADYDNKWVSIFSSDGKFKTKIGSG-------------KLMGPKGVSVDRNGHIIVVD---NKACCVFifqPNG 481
Cdd:cd14953   141 AAGNLYVADTGNHRIRKITPDGVVTTVAGTGgagyagdgpataaQFNNPTGVAVDAAGNLYVADrgnHRIRKIT---PDG 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 482 KIVTRFGSRGNGDR--------QFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFM----LKFGSNGEGNG----QFN 545
Cdd:cd14953   218 VVTTVAGTGTAGFSgdggataaQLNNPTGVAVDAAGNLYVADSGNHRIRKITPAGVVTtvagGGAGFSGDGGPatsaQFN 297
                         250       260
                  ....*....|....*....|...
gi 1189131358 546 APTGVAVDSNGNIIVADWGNSRI 568
Cdd:cd14953   298 NPTGVAVDAAGNLYVADTGNNRI 320
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
405-617 1.90e-27

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 112.04  E-value: 1.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 405 PGQLQRPTGVAVHPSGDIIIADYDNKWVSIFS-SDGKFkTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKI 483
Cdd:COG4257    13 PAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDpATGEF-TEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 484 VTRFGSRGNGdrqfAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGqfnaPTGVAVDSNGNIIVADW 563
Cdd:COG4257    92 ITTFALPGGG----SNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPLPTGGAG----PYGIAVDPDGNLWVTDF 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1189131358 564 GNSRIQVFDGSGSFLSYINTSAdPLYGPQGLALTSDGHVVVADSGNHcfKVYRY 617
Cdd:COG4257   164 GANAIGRIDPDTGTLTEYALPT-PGAGPRGLAVDPDGNLWVADTGSG--RIGRF 214
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
491-615 2.05e-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: 111.61  E-value: 2.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 491 GNGDRQFAGPHFAAVnSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQV 570
Cdd:cd14963     3 GPFGDPLNKPMGVAV-SDGRIYVADTNNHRVQVFDYEGKFKKSFGGPGTGPGEFKYPYGIAVDSDGNIYVADLYNGRIQV 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1189131358 571 FDGSGSFLSYINTSAD--PLYGPQGLALtSDGHVVVADSGNHCFKVY 615
Cdd:cd14963    82 FDPDGKFLKYFPEKKDrvKLISPAGLAI-DDGKLYVSDVKKHKVIVF 127
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
36-157 1.04e-26

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: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  36 HKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQ 115
Cdd:cd20482     1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1189131358 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 5.63e-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: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 352 GTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKW 431
Cdd:cd14955   147 GSFGSGDGQFNSPTGIAVDSAGNVYVADTGNNRIQKFTSTGTFLTKWGSEGSGDGQFNAPYGIAVDSAGNVYVADTGNNR 226
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1189131358 432 VSIFSSDGKFKTKIGS-----GKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP 479
Cdd:cd14955   227 IQKFDSSGTFITKWGSegsgdGQFNSPSGIAVDSAGNVYVADSGNNRIQKFAP 279
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
450-615 3.82e-25

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: 105.36  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 450 LMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRG-------------------------------NGDRQFA 498
Cdd:cd14962    11 LTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGpnrfvspigvaidangnlyvsdaelgkvfvfDRDGKFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 499 G----------PHFAAVNS-NNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSR 567
Cdd:cd14962    91 RaigagalfkrPTGIAVDPaGKRLYVVDTLAHKVKVFDLDGRLLFDIGKRGSGPGEFNLPTDLAVDRDGNLYVTDTMNFR 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1189131358 568 IQVFDGSGSFLSYINTSADPlYG----PQGLALTSDGHVVVADSGNHCFKVY 615
Cdd:cd14962   171 VQIFDADGKFLRSFGERGDG-PGsfarPKGIAVDSEGNIYVVDAAFDNVQIF 221
IG_FLMN smart00557
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ...
200-296 1.92e-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: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  200 ASETVATGEGLRQTIIGQPMSVTITTKDKdgelcktGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:smart00557   1 ASKVKASGPGLEKGVVGEPAEFTVDTRDA-------GGGELEVEVTGPSGKKVPVEVKDNGDGTYTVSYTPTEPGDYTVT 73
                           90
                   ....*....|....*..
gi 1189131358  280 LRLYDQHIRGSPFKLKV 296
Cdd:smart00557  74 VKFGGEHIPGSPFTVKV 90
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
359-580 6.90e-24

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 101.63  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 359 GEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKsRFGIrgrsPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFS- 436
Cdd:COG4257    56 GGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDpKTGEIT-TFAL----PGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDp 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 437 SDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFgsrgNGDRQFAGPHFAAVNSNNEIIITDF 516
Cdd:COG4257   131 ATGEVTEFPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEY----ALPTPGAGPRGLAVDPDGNLWVADT 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131358 517 HNHSVKVFN----QEGEFMLKFGSNGegngqfnaPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSY 580
Cdd:COG4257   207 GSGRIGRFDpktgTVTEYPLPGGGAR--------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 1189131358 200 ASETVATGEGLRQTIIGQPMSVTITTKDKDGELcktgnaylTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLS 279
Cdd:pfam00630   4 ASKVKASGPGLEPGVVGKPAEFTVDTRDAGGEG--------EVEVTGPDGSPVPVEVTDNGDGTYTVSYTPTEPGDYTVS 75
                          90
                  ....*....|....
gi 1189131358 280 LRLYDQHIRGSPFK 293
Cdd:pfam00630  76 VKFNGQHIPGSPFK 89
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
361-610 2.98e-21

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: 93.43  E-value: 2.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 361 FTNL---QGVAASTNGKILIADS-NNQCVQIFSN-DGQFKSRFGirgrspgQLQRPTGVAVHPSGDIIIADYDNKWVSIF 435
Cdd:cd14952     6 FTGLdgpGGVAVDAAGNVYVADSgNNRVLKLAAGsTTQTVLPFT-------GLYQPQGVAVDAAGTVYVTDFGNNRVLKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 436 SSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNkaccvfifqPNGKIVTRfgsRGNGDRQ----FAG---PHFAAVNSN 508
Cdd:cd14952    79 AAGSTTQTVLPFTGLNDPTGVAVDAAGNVYVADT---------GNNRVLKL---AAGSNTQtvlpFTGlsnPDGVAVDGA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 509 NEIIITDFHNHSVkvfnqegeFMLKFGSNGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRIQVFDgSGSflsyiNTSA 585
Cdd:cd14952   147 GNVYVTDTGNNRV--------LKLAAGSTTQTVLPFtglNSPSGVAVDTAGNVYVTDHGNNRVLKLA-AGS-----TTPT 212
                         250       260
                  ....*....|....*....|....*....
gi 1189131358 586 ----DPLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14952   213 vlpfTGLNGPLGVAVDAAGNVYVADRGND 241
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
455-613 1.54e-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: 92.33  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 455 GVSVDRNGHIIVV-------DNKACCVFIFQPNGKI----VTRFGSRGN-----GDRQFAGPHFAAVNSNNEIIITDFHN 518
Cdd:cd14958    17 GVAVDSLGNGVVFhrggrvwDANSFDANVYVFKGPIeedtILVFDPDGGflrswGAGLFYMPHGLTIDPDGNIWVTDVGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 519 HSVKVFNQEGE--FMLKFGSN---GEGNGQFNAPTGVAVDSNGNIIVAD-WGNSRIQVFDGSGSFLSYINTSADPLyG-- 590
Cdd:cd14958    97 HQVFKFDPEGKllPLLTLGERgepGSDQTHFCKPTDVAVAPDGDIFVADgYCNSRIVKFSPDGKLLKSWGEPGSGP-Gqf 175
                         170       180
                  ....*....|....*....|....*...
gi 1189131358 591 --PQGLALTSDGHVVVADSGNH---CFK 613
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 5.25e-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: 5.25e-20
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1189131358   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) ...
533-615 3.17e-19

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


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 88.11  E-value: 3.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 533 KFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINT---SADPLYGPQGLALTSDGHVVVADSGN 609
Cdd:cd14956     1 SWGGRGSGPGQFKDPRGIAVDADDNVYVADARNGRIQVFDKDGTFLRRFGTtgdGPGQFGRPRGLAVDKDGWLYVADYWG 80

                  ....*.
gi 1189131358 610 HCFKVY 615
Cdd:cd14956    81 DRIQVF 86
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
385-572 4.73e-19

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: 88.09  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 385 VQIFSNDGQFKSRFGirgrsPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMG----------PK 454
Cdd:cd14958    57 ILVFDPDGGFLRSWG-----AGLFYMPHGLTIDPDGNIWVTDVGLHQVFKFDPEGKLLPLLTLGERGEpgsdqthfckPT 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 455 GVSVDRNGHIIVVD---NKacCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEF- 530
Cdd:cd14958   132 DVAVAPDGDIFVADgycNS--RIVKFSPDGKLLKSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFl 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 531 -------------------------------------------MLK------FGSNGEGNGQFNAPTGVAVDSNGNIIVA 561
Cdd:cd14958   210 tewtnpelgrpyalaidpdgllyvvdgpprlnrslpvrgfvirIGKglilgrFGPGGKAPGQFQNPHDIAVDSGGDIYVG 289
                         250
                  ....*....|.
gi 1189131358 562 DWGNSRIQVFD 572
Cdd:cd14958   290 ELGPNRVQKFV 300
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
487-611 5.14e-19

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


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 88.36  E-value: 5.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 487 FGSRGNGDR--QFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEfMLKFGSNGE-----GNG---QFNAPTGVAVDSNG 556
Cdd:cd14953    10 AGFSGGGGTaaRFNSPSGVAVDAAGNLYVADRGNHRIRKITPDGV-VTTVAGTGTagfadGGGaaaQFNTPSGVAVDAAG 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189131358 557 NIIVADWGNSRI---------QVFDGSGS--FLSYINTSADPLYGPQGLALTSDGHVVVADSGNHC 611
Cdd:cd14953    89 NLYVADTGNHRIrkitpdgvvSTLAGTGTagFSDDGGATAAQFNYPTGVAVDAAGNLYVADTGNHR 154
NHL_PAL_like cd14958
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
367-524 5.93e-19

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: 87.70  E-value: 5.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 367 VAASTNGKILIAD--SNNQCVQiFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTK 444
Cdd:cd14958   133 VAVAPDGDIFVADgyCNSRIVK-FSPDGKLLKSWGEPGSGPGQFNLPHSIALDEDGRVYVADRENGRIQVFDADGKFLTE 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 445 IGSGKLMGPKGVSVDRNGHIIVVD-------NKACCVFIFQPN-GKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDF 516
Cdd:cd14958   212 WTNPELGRPYALAIDPDGLLYVVDgpprlnrSLPVRGFVIRIGkGLILGRFGPGGKAPGQFQNPHDIAVDSGGDIYVGEL 291

                  ....*...
gi 1189131358 517 HNHSVKVF 524
Cdd:cd14958   292 GPNRVQKF 299
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
522-610 7.79e-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: 7.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 522 KVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADP---LYGPQGLALTS 598
Cdd:cd14954     1 RDYRAKGRPLLSFGKEGSKDGELCRPWGVAVDKDGRIIVADRSNNRVQVFDPDGKFLRKFGSYGSRdgqFDRPAGVAVNS 80
                          90
                  ....*....|..
gi 1189131358 599 DGHVVVADSGNH 610
Cdd:cd14954    81 RGRIIVADKDNH 92
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
346-435 2.87e-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: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 346 DLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIA 425
Cdd:cd14954   196 QFLRFFGSEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVV 275
                          90
                  ....*....|
gi 1189131358 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 1.92e-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: 1.92e-17
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1189131358   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 4.27e-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: 4.27e-17
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1189131358   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 8.39e-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: 78.09  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 342 PIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGD 421
Cdd:cd14956   181 DNDGAFLRKWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGSPGTGPGQFKNPWGVVVDADGT 260

                  ....*...
gi 1189131358 422 IIIADYDN 429
Cdd:cd14956   261 VYVADSNN 268
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
361-568 1.46e-13

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: 70.70  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 361 FTNL---QGVAASTNGKILIADS-NNQCVQIfsndgqfksrfgIRGRSP------GQLQRPTGVAVHPSGDIIIADYDNK 430
Cdd:cd14952    48 FTGLyqpQGVAVDAAGTVYVTDFgNNRVLKL------------AAGSTTqtvlpfTGLNDPTGVAVDAAGNVYVADTGNN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 431 WVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDnkaccvfifqPNGKIVTRFGSRGNGDRQ--FAG---PHFAAV 505
Cdd:cd14952   116 RVLKLAAGSNTQTVLPFTGLSNPDGVAVDGAGNVYVTD----------TGNNRVLKLAAGSTTQTVlpFTGlnsPSGVAV 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131358 506 NSNNEIIITDFHNHSVkvfnqegefmLKF--GSNGEGNGQF---NAPTGVAVDSNGNIIVADWGNSRI 568
Cdd:cd14952   186 DTAGNVYVTDHGNNRV----------LKLaaGSTTPTVLPFtglNGPLGVAVDAAGNVYVADRGNDRV 243
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
455-619 2.08e-10

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 61.25  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 455 GVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQE-GEFM-- 531
Cdd:COG3391    26 AALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLAtGKVVat 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 532 LKFGSNgegngqfnaPTGVAVDSNGN-IIVADWGNSRIQVFDG-SGSFLSYINTSAdplyGPQGLALTSDG-HVVVADSG 608
Cdd:COG3391   106 IPVGGG---------PRGLAVDPDGGrLYVADSGNGRVSVIDTaTGKVVATIPVGA----GPHGIAVDPDGkRLYVANSG 172
                         170
                  ....*....|.
gi 1189131358 609 NHcfKVYRYLQ 619
Cdd:COG3391   173 SN--TVSVIVS 181
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 1189131358    1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:smart00336  14 AEFFCEECGALLCRTCDEAEHRGHTVVLL 42
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
444-617 2.90e-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: 58.36  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 444 KIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNgdrqfaGPHFAAVNSNNEIIITDfHNHSVKV 523
Cdd:COG3386     1 KLADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPSG------RPNGLAFDPDGRLLVAD-HGRGLVR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 524 FN-QEGEFMLKFGSNGEGNGQFNaptGVAVDSNGNIIVAD----WGNSRIQVFDGSGSflsyINTSADPLYGPQGLALTS 598
Cdd:COG3386    74 FDpADGEVTVLADEYGKPLNRPN---DGVVDPDGRLYFTDmgeyLPTGALYRVDPDGS----LRVLADGLTFPNGIAFSP 146
                         170       180
                  ....*....|....*....|
gi 1189131358 599 DG-HVVVADSGNHcfKVYRY 617
Cdd:COG3386   147 DGrTLYVADTGAG--RIYRF 164
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
366-578 5.13e-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: 57.59  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 366 GVAASTNGKILIADSNNQCVQIFSNDGQFKSRFgirgRSPGQlqRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKI 445
Cdd:COG3386    12 GPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVF----AEPSG--RPNGLAFDPDGRLLVADHGRGLVRFDPADGEVTVLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 446 GSG--KLMGPKGVSVDRNGHIIVVDnkaccVFIFQPNGKIVtRFGSRGNGDRQFAGPHFA---AVNSNNEI-IITDFHNH 519
Cdd:COG3386    86 DEYgkPLNRPNDGVVDPDGRLYFTD-----MGEYLPTGALY-RVDPDGSLRVLADGLTFPngiAFSPDGRTlYVADTGAG 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189131358 520 SVKVF--NQEGEFMLK--FGSNGEGNGqfnAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFL 578
Cdd:COG3386   160 RIYRFdlDADGTLGNRrvFADLPDGPG---GPDGLAVDADGNLWVALWGGGGVVRFDPDGELL 219
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
345-572 7.13e-09

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 56.63  E-value: 7.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 345 DDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIII 424
Cdd:COG3391     5 SSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 425 ADYDNKWVSIF-SSDGKFKTKIGSGKlmGPKGVSVDRNG-HIIVVDNKACCVFIF-QPNGKIVTRFGSrGNGdrqfagPH 501
Cdd:COG3391    85 ANSGSGRVSVIdLATGKVVATIPVGG--GPRGLAVDPDGgRLYVADSGNGRVSVIdTATGKVVATIPV-GAG------PH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 502 FAAVNS-NNEIIITDFHNHS----VKVFN-QEGEFM--LKFGSNgegngqfnaPTGVAVDSNGNIIV--------ADWGN 565
Cdd:COG3391   156 GIAVDPdGKRLYVANSGSNTvsviVSVIDtATGKVVatIPVGGG---------PVGVAVSPDGRRLYvanrgsntSNGGS 226

                  ....*..
gi 1189131358 566 SRIQVFD 572
Cdd:COG3391   227 NTVSVID 233
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
539-617 8.73e-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: 8.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 539 EGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYG-PQGLALTSDGHVVVADSGNHcfKVYRY 617
Cdd:cd14962     6 RPKEALTRPYGVAADGRGRIYVADTGRGAVFVFDLPNGKVFVIGNAGPNRFVsPIGVAIDANGNLYVSDAELG--KVFVF 83
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
347-435 1.06e-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: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 347 LIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSR----------------------------- 397
Cdd:cd14963   133 LLLEFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFIKElngspdgksgfvnprgiavdpdgnlyvvd 212
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189131358 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 1.83e-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: 1.83e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1189131358   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHK 37
Cdd:cd19796    12 LRLYCDTCSVPICRECTMGEHRGHSFIYLQEAVQDSK 48
zf-B_box pfam00643
B-box zinc finger;
1-29 3.97e-08

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 49.39  E-value: 3.97e-08
                          10        20
                  ....*....|....*....|....*....
gi 1189131358   1 MEFYCQSCETAMCRECTEGEHAEHPTVPL 29
Cdd:pfam00643  14 LTLYCNDCQELLCEECSVGEHRGHTVVPL 42
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
404-617 7.36e-08

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


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 54.13  E-value: 7.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 404 SPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKlMGPKGVSVDRNGHIIVVDNKACcVFIFQPNGKI 483
Cdd:COG3386     3 ADAGFRLGEGPVWDPDGRLYWVDIPGGRIHRYDPDGGAVEVFAEPS-GRPNGLAFDPDGRLLVADHGRG-LVRFDPADGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 484 VTRFGSRGngDRQFAGPHFAAVNSNNEIIITDFHNH----SVKVFNQEGEFMLKFGSngegngqFNAPTGVAVDSNGNI- 558
Cdd:COG3386    81 VTVLADEY--GKPLNRPNDGVVDPDGRLYFTDMGEYlptgALYRVDPDGSLRVLADG-------LTFPNGIAFSPDGRTl 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189131358 559 IVADWGNSRIQVFD--GSGSfLS----YINTSADPlYGPQGLALTSDGHVVVADSGNHCfkVYRY 617
Cdd:COG3386   152 YVADTGAGRIYRFDldADGT-LGnrrvFADLPDGP-GGPDGLAVDADGNLWVALWGGGG--VVRF 212
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
544-571 1.44e-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: 1.44e-07
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 544 FNAPTGVAVDSNGNIIVADWGNSRIQVF 571
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
507-617 2.40e-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: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 507 SNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVD-SNGNIIVADWGNSRIQVFD-GSGSFLSYINTS 584
Cdd:pfam17170  52 VDDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQINDFIIDkSNNSIYILDFMQNKILTYDlDGYSFIGEINLD 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1189131358 585 ADP-----------LYGPQGLA--LTSDGHVVVADS-GNHCFKVYRY 617
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 ...
588-615 3.95e-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: 3.95e-06
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 588 LYGPQGLALTSDGHVVVADSGNHCFKVY 615
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
497-524 6.02e-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: 43.16  E-value: 6.02e-06
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 497 FAGPHFAAVNSNNEIIITDFHNHSVKVF 524
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 9.31e-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: 9.31e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1189131358   1 MEFYCQSCETAMCREC-TEGEHAEHPTVPL 29
Cdd:cd19756    10 LKLFCETCQELVCVLClLSGEHRGHKVVPL 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
356-616 1.12e-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: 47.71  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 356 RNKGEFTNLQGVAASTNGKILIADSNNQCVQIFS-NDGQFKSRFGirgrspGQLQRPTGVAVHPSGDIIIADYDNKWVSI 434
Cdd:cd00200    46 TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDlETGECVRTLT------GHTSYVSSVAFSPDGRILSSSSRDKTIKV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 435 FS-SDGKFKTKIgSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQP-NGKIVTRFGSrgngdrqfagpHFAAVNS----- 507
Cdd:cd00200   120 WDvETGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLrTGKCVATLTG-----------HTGEVNSvafsp 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 508 NNEIIITDFHNHSVKVFNQEGEFMLKfgsngEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDG-SGSFLSyintsad 586
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTGKCLG-----TLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLrTGECVQ------- 255
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1189131358 587 PLYGPQG----LALTSDGHVVVADSGNHCFKVYR 616
Cdd:cd00200   256 TLSGHTNsvtsLAWSPDGKRLASGSADGTIRIWD 289
DUF5128 pfam17170
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ...
371-555 1.57e-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: 47.32  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 371 TNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTgvavhpsgDIIIADYDNkwvSIFSSDgKFKTKIGSGKL 450
Cdd:pfam17170  52 VDDRIFVFDSNTNNLFVFDKKGKFVRQIGAQGNGPGEYLQIN--------DFIIDKSNN---SIYILD-FMQNKILTYDL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 451 MGPKGVSVDRnghiivVDNKACCVFIFQPNGKIvtrFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNhsvkvfnqegEF 530
Cdd:pfam17170 120 DGYSFIGEIN------LDLLPSDCCQLDKGKLA---FDSSGFDDGKRSGFYLVITDELGNIISGFFPA----------EF 180
                         170       180
                  ....*....|....*....|....*
gi 1189131358 531 MLKFGSNgegngqfNAPTGVAVDSN 555
Cdd:pfam17170 181 TLGILFN-------SSVPFYEYGDN 198
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
372-572 2.10e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 47.92  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  372 NGKILIA----------DSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQrPTGVAVHPSGD-IIIADYDNKwvSIFSSDgk 440
Cdd:PLN02919   694 NEKVYIAmagqhqiweyNISDGVTRVFSGDGYERNLNGSSGTSTSFAQ-PSGISLSPDLKeLYIADSESS--SIRALD-- 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  441 FKTKiGSGKLMGpkgvsvdrnGHIIVVDNkaccvfIFQpngkivtrFGSR-GNGDR-QFAGPHFAAVNSNNEIIITDFHN 518
Cdd:PLN02919   769 LKTG-GSRLLAG---------GDPTFSDN------LFK--------FGDHdGVGSEvLLQHPLGVLCAKDGQIYVADSYN 824
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131358  519 HSVKVFNQEGEFMLKFGSNGEGN--------GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 572
Cdd:PLN02919   825 HKIKKLDPATKRVTTLAGTGKAGfkdgkalkAQLSEPAGLALGENGRLFVADTNNSLIRYLD 886
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
547-610 2.16e-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: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189131358 547 PTGVAVDSNGNIIVADWGNSRIQVFD----------GSGSFLSYINTSAdpLYGPQGLALTSDGHVVVADSGNH 610
Cdd:cd14951   198 PLGVAALPDGSVYVADTYNHKIKRVDpatgevstlaGTGKAGYKDLEAQ--FSEPSGLVVDGDGRLYVADTNNH 269
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
34-190 2.88e-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: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  34 EQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHstfdELQKTLNVRksvllmELEVNyGLKHKV-- 111
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR----DLKDMLDVK------ERKIN-VLQKKIen 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 112 LQSQL---DTLLQG-QESIKSC---SNFTAQALnhGTETEVLLVKKQMSEKLNEladqdfplhPRENDQLDFIVETEGLK 184
Cdd:pfam10174 406 LQEQLrdkDKQLAGlKERVKSLqtdSSNTDTAL--TTLEEALSEKERIIERLKE---------QREREDRERLEELESLK 474

                  ....*.
gi 1189131358 185 KSIHNL 190
Cdd:pfam10174 475 KENKDL 480
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
411-616 4.43e-05

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


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 46.05  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 411 PTGVAVHPSGDIIIA--DYDNKWVSIFS---SDGKFkTKIGSGKLMG--PKGVSVDRNGHIIVVDN---KACCVFIFQPN 480
Cdd:COG2706    47 PSFLALSPDGRFLYAvnEVDDGGVSAFRidpADGTL-TLLNTVSSGGasPCHLSVDPDGRFLFVANyggGSVSVFPIDAD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 481 GKI------VTRFGSRGNGDRQ-FAGPHFAAVN-SNNEIIITDFHNHSVKVFN---------QEGEFMLKFGS------- 536
Cdd:COG2706   126 GSLgepvqvIQHEGSGPNPERQeGPHAHSVVFDpDGRFLYVPDLGTDRIYVYRldpatgklpEPPEVSLPPGSgprhlaf 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 537 --NG-------------------EGNGQF----------------NAPTGVAVDSNGN-IIVADWGNSRIQVF-----DG 573
Cdd:COG2706   206 hpNGrfayvineldstvsvyaydAATGTLtliqtvstlpedftgeNWAADIHISPDGRfLYVSNRGHNSIAVFaidadGG 285
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1189131358 574 SGSFLSYINTSADplyGPQGLALTSDG-HVVVADSGNHCFKVYR 616
Cdd:COG2706   286 KLTLVGHVPTGGK---WPRDFAIDPDGrFLLVANQKSDNITVFR 326
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
1-37 4.95e-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: 4.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1189131358   1 MEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHK 37
Cdd:cd19769    10 LELFCRTDQMCICELCAKEEHRGHDVVTVEEEREKKE 46
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
504-572 6.01e-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: 45.65  E-value: 6.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189131358 504 AVNSNNEIIITDFHNHSVKVFN---QEGEFMLKFGSNGEGN--GQFNAPTGVAVDSNGNIIVADWGNSRIQVFD 572
Cdd:cd14951   202 AALPDGSVYVADTYNHKIKRVDpatGEVSTLAGTGKAGYKDleAQFSEPSGLVVDGDGRLYVADTNNHRIRRLD 275
Bbox2_TRIM56_C-V cd19789
B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar ...
1-33 6.35e-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: 6.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1189131358   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 7.78e-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: 7.78e-05
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 408 LQRPTGVAVHPSGDIIIADYDNKWVSIF 435
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
Bbox2_TRIM45_C-X cd19785
B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar ...
3-32 2.49e-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: 2.49e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1189131358   3 FYCQSCETAMCRECTEGEHAEHPTVPLKDV 32
Cdd:cd19785    14 LFCETCDKPVCRDCVLVEHRGHQCDFTSDV 43
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
361-618 2.86e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 44.07  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  361 FTNLQGVAASTNGKIL-IADSNN----------QCVQIFSNDGQFKSRFgiRGRSPGQLQ---RPTGVAVHPSGDII--- 423
Cdd:PLN02919   623 FNRPQGLAYNAKKNLLyVADTENhalreidfvnETVRTLAGNGTKGSDY--QGGKKGTSQvlnSPWDVCFEPVNEKVyia 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  424 ------IADYD--NKWVSIFSSDGKFKTKIGSG----KLMGPKGVSVDRN-GHIIVVDNKACCVfifqpngkivTRFGSR 490
Cdd:PLN02919   701 magqhqIWEYNisDGVTRVFSGDGYERNLNGSSgtstSFAQPSGISLSPDlKELYIADSESSSI----------RALDLK 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  491 GNGDRQFAG--PHFaavnSNNeiiitdfhnhsvkvfnqegefMLKFGSN-GEG-NGQFNAPTGVAVDSNGNIIVADWGNS 566
Cdd:PLN02919   771 TGGSRLLAGgdPTF----SDN---------------------LFKFGDHdGVGsEVLLQHPLGVLCAKDGQIYVADSYNH 825
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189131358  567 RIQVFDGSGSFLSYINTS-----------ADPLYGPQGLALTSDGHVVVADSGNhcfKVYRYL 618
Cdd:PLN02919   826 KIKKLDPATKRVTTLAGTgkagfkdgkalKAQLSEPAGLALGENGRLFVADTNN---SLIRYL 885
NHL pfam01436
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ...
361-388 3.04e-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: 3.04e-04
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 361 FTNLQGVAASTNGKILIADSNNQCVQIF 388
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
408-468 3.32e-04

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: 43.33  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189131358 408 LQRPTGVAVHPSGDIIIADYDN----------KWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVD 468
Cdd:cd14951   195 LQHPLGVAALPDGSVYVADTYNhkikrvdpatGEVSTLAGTGKAGYKDLEAQFSEPSGLVVDGDGRLYVAD 265
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
344-388 3.57e-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: 3.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1189131358 344 EDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIF 388
Cdd:cd14954   241 DGEFLCSFGTEGNGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQVF 285
ScyE_fam NF033206
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ...
544-605 4.89e-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: 4.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131358 544 FNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSfLSYI------NTSADPLYGPQGLALTSDGHVVVA 605
Cdd:NF033206  249 FTGLTDLAFDPDGNLYVLELAGGGLLKGDPTGS-LIRIapdgtrTTLLDGLELPTGLAVGPDGTLYVT 315
WD40 COG2319
WD40 repeat [General function prediction only];
366-616 6.90e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.21  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 366 GVAASTNGKILIADSNNQCVQIFS-NDGQFKSRFgirgrsPGQLQRPTGVAVHPSGDIII-ADYDNKwVSIFSSDGKFKT 443
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDlATGKLLRTL------TGHTGAVRSVAFSPDGKLLAsGSADGT-VRLWDLATGKLL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 444 KIGSGKLMGPKGVSVDRNGHIIVV---DNKaccVFIFQPN-GKIVTRFGSrgngdrqfagpHFAAVNS-----NNEIIIT 514
Cdd:COG2319   240 RTLTGHSGSVRSVAFSPDGRLLASgsaDGT---VRLWDLAtGELLRTLTG-----------HSGGVNSvafspDGKLLAS 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 515 DFHNHSVKVFN-QEGEFMLKFgsngegNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLsyINTSADPLYGPQG 593
Cdd:COG2319   306 GSDDGTVRLWDlATGKLLRTL------TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL--LRTLTGHTGAVTS 377
                         250       260
                  ....*....|....*....|...
gi 1189131358 594 LALTSDGHVVVADSGNHCFKVYR 616
Cdd:COG2319   378 VAFSPDGRTLASGSADGTVRLWD 400
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
508-617 8.69e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 42.53  E-value: 8.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358  508 NNEIIITDFHNHSVKVFNQEGEFMLKFGSNGE--------GNGQFNAPTGVAVDSNGNII-VA----------DWGNSRI 568
Cdd:PLN02919   579 NNRLFISDSNHNRIVVTDLDGNFIVQIGSTGEeglrdgsfEDATFNRPQGLAYNAKKNLLyVAdtenhalreiDFVNETV 658
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189131358  569 QVFDGSGS----FLSYINTSADPLYGPQGLALTS-DGHVVVADSGNHcfKVYRY 617
Cdd:PLN02919   659 RTLAGNGTkgsdYQGGKKGTSQVLNSPWDVCFEPvNEKVYIAMAGQH--QIWEY 710
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
546-575 1.12e-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: 1.12e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1189131358 546 APTGVAVDSNGNIIVADWGNSRIQVFDGSG 575
Cdd:pfam08450 185 RPDGMAVDAEGNVWVARWGGGKVVRFDPDG 214
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
343-487 1.97e-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: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 343 IEDDLIFRVGTKGRNKGEFTNLQ----GVAASTNGKILIADSNNQCVQIFSNDGQFK---SRFGIRGRSP---------- 405
Cdd:COG3386    26 IPGGRIHRYDPDGGAVEVFAEPSgrpnGLAFDPDGRLLVADHGRGLVRFDPADGEVTvlaDEYGKPLNRPndgvvdpdgr 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 406 ---------------------GQLQR-------PTGVAVHPSGDI-IIADYDNKWVSIF--SSDGK-------FKTKIGS 447
Cdd:COG3386   106 lyftdmgeylptgalyrvdpdGSLRVladgltfPNGIAFSPDGRTlYVADTGAGRIYRFdlDADGTlgnrrvfADLPDGP 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1189131358 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 2.05e-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: 2.05e-03
                          10        20
                  ....*....|....*....|....*...
gi 1189131358 450 LMGPKGVSVDRNGHIIVVDNKACCVFIF 477
Cdd:pfam01436   1 FNRPHGVAVDSNGDIYVADSENHRVQVF 28
WD40 COG2319
WD40 repeat [General function prediction only];
399-616 5.60e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 399 GIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVV---DNKaccVF 475
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASgsaDGT---VR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131358 476 IFQP-NGKIVTRFgsRGNGDRQFAgphfAAVNSNNEIIITDFHNHSVKVFN-QEGEFMLKFgsngegNGQFNAPTGVAVD 553
Cdd:COG2319   146 LWDLaTGKLLRTL--TGHSGAVTS----VAFSPDGKLLASGSDDGTVRLWDlATGKLLRTL------TGHTGAVRSVAFS 213
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189131358 554 SNGNIIVADWGNSRIQVFD-GSGSFLSYINTSADPLYgpqGLALTSDGHVVVADSGNHCFKVYR 616
Cdd:COG2319   214 PDGKLLASGSADGTVRLWDlATGKLLRTLTGHSGSVR---SVAFSPDGRLLASGSADGTVRLWD 274
NHL-2_like cd14951
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ...
591-610 8.99e-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: 8.99e-03
                          10        20
                  ....*....|....*....|
gi 1189131358 591 PQGLALTSDGHVVVADSGNH 610
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 9.84e-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: 9.84e-03
                          10        20
                  ....*....|....*....|....*.
gi 1189131358   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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