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Conserved domains on  [gi|537139217|gb|ERE67402|]
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tripartite motif-containing protein 54 [Cricetulus griseus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 17-79 1.03e-31

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 115.26  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537139217   17 SLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 201-243 2.08e-27

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


:

Pssm-ID: 380891  Cd Length: 43  Bit Score: 103.23  E-value: 2.08e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTI 243
Cdd:cd19833    1 LMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTV 43
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 247-350 3.59e-03

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.


The actual alignment was detected with superfamily member smart00502:

Pssm-ID: 475168  Cd Length: 127  Bit Score: 37.24  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217   247 QKSELSDGIAMLVAGNDRVQAVITQMEEVCQTIEDNSRRQKQLLNQRFETLCAVLEERKGELLQALAREQEEKLQRVRGL 326
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100
                   ....*....|....*....|....
gi 537139217   327 IrqygDHLEVSSKLVESAIQSMEE 350
Cdd:smart00502  81 L----ESLTQKQEKLSHAINFTEE 100
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 17-79 1.03e-31

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 115.26  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537139217   17 SLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 19-90 7.08e-29

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 110.56  E-value: 7.08e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGIYLFD 90
Cdd:COG0484    3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 19-82 1.06e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 116.01  E-value: 1.06e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYG 70
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 201-243 2.08e-27

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


Pssm-ID: 380891  Cd Length: 43  Bit Score: 103.23  E-value: 2.08e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTI 243
Cdd:cd19833    1 LMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTV 43
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 19-82 3.33e-26

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 108.84  E-value: 3.33e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217   19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQFG 65
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 19-71 8.53e-24

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 93.76  E-value: 8.53e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSD 71
Cdd:cd06257    3 YDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
16-74 1.87e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 92.68  E-value: 1.87e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217    16 TSLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGD-IQAAEFFKEINTAHAVLSDPTK 74
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
zf-B_box pfam00643
B-box zinc finger;
199-240 3.12e-07

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 46.70  E-value: 3.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 537139217  199 QHLMCEEHEDEKINIYCLSCEVPTCSLCKVfGAHKDCEVAPL 240
Cdd:pfam00643   2 KERLCPEHEEEPLTLYCNDCQELLCEECSV-GEHRGHTVVPL 42
BBOX smart00336
B-Box-type zinc finger;
201-240 6.88e-06

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 42.71  E-value: 6.88e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 537139217   201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFgAHKDCEVAPL 240
Cdd:smart00336   4 PKCDSHGDEPAEFFCEECGALLCRTCDEA-EHRGHTVVLL 42
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 247-350 3.59e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 37.24  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217   247 QKSELSDGIAMLVAGNDRVQAVITQMEEVCQTIEDNSRRQKQLLNQRFETLCAVLEERKGELLQALAREQEEKLQRVRGL 326
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100
                   ....*....|....*....|....
gi 537139217   327 IrqygDHLEVSSKLVESAIQSMEE 350
Cdd:smart00502  81 L----ESLTQKQEKLSHAINFTEE 100
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 265-359 4.90e-03

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: 36.75  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217 265 VQAVITQMEEVCQTIEDNSRRQKQLLNQRFETLCAVLEERKGELLQALAR---EQEEKLQRVRGLIRQYGDHLEVSSKLV 341
Cdd:cd20482   19 LRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESiynAKQLSLNEQQQKLQETIEKIQQGCEFT 98

                         90
                 ....*....|....*...
gi 537139217 342 ESAIQSMEEPQMALYLQQ 359
Cdd:cd20482   99 ERLLKHGSETEVLLFKKL 116
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 17-79 1.03e-31

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 115.26  E-value: 1.03e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537139217   17 SLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 19-90 7.08e-29

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 110.56  E-value: 7.08e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGIYLFD 90
Cdd:COG0484    3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 19-82 1.06e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 116.01  E-value: 1.06e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYG 70
Bbox2_MuRF3_C-II cd19833
B-box-type 2 zinc finger found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 201-243 2.08e-27

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


Pssm-ID: 380891  Cd Length: 43  Bit Score: 103.23  E-value: 2.08e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTI 243
Cdd:cd19833    1 LMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTV 43
PRK14297 PRK14297
molecular chaperone DnaJ;
19-96 3.15e-26

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 109.49  E-value: 3.15e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGIYLFDHFGEDG 96
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAGGFGSGG 84
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 19-82 3.33e-26

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 108.84  E-value: 3.33e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217   19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQFG 65
Bbox2_MuRF1_C-II cd19831
B-box-type 2 zinc finger found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
 200-241 2.79e-25

B-box-type 2 zinc finger found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins; MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380889  Cd Length: 43  Bit Score: 97.42  E-value: 2.79e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 537139217 200 HLMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLP 241
Cdd:cd19831    2 HPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQ 43
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 18-82 6.39e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 105.65  E-value: 6.39e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537139217  18 LYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14277   7 YYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFG 71
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 19-86 2.42e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 103.69  E-value: 2.42e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGL 74
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 19-86 5.44e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 102.96  E-value: 5.44e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGV 73
Bbox2_MuRF cd19788
B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This ...
 202-240 5.52e-24

B-box-type 2 zinc finger found in muscle-specific RING finger protein (MuRF) family; This family corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380846  Cd Length: 39  Bit Score: 93.68  E-value: 5.52e-24
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 537139217 202 MCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19788    1 MCEEHEEEKINIYCLTCEVPTCSMCKVFGAHKDCEVAPL 39
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 19-76 6.00e-24

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 94.30  E-value: 6.00e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKR 76
Cdd:COG5407    3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 19-71 8.53e-24

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 93.76  E-value: 8.53e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSD 71
Cdd:cd06257    3 YDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
Bbox2_MuRF2_C-II cd19832
B-box-type 2 zinc finger found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
 202-245 9.67e-24

B-box-type 2 zinc finger found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins; MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signalling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380890  Cd Length: 45  Bit Score: 93.21  E-value: 9.67e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 537139217 202 MCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYK 245
Cdd:cd19832    2 MCEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQ 45
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 19-82 1.65e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 101.28  E-value: 1.65e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14278   6 YGLLGVSRNASDAEIKRAYRKLARELHPDVNP-DEEAQEKFKEISVAYEVLSDPEKRRIVDLGG 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 19-87 1.77e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 101.46  E-value: 1.77e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGIY 87
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPF 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
16-74 1.87e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 92.68  E-value: 1.87e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217    16 TSLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGD-IQAAEFFKEINTAHAVLSDPTK 74
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
PRK14289 PRK14289
molecular chaperone DnaJ;
19-86 1.18e-22

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 99.14  E-value: 1.18e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGV 75
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 19-82 1.66e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 95.61  E-value: 1.66e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQFG 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 17-86 4.43e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 94.29  E-value: 4.43e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217  17 SLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14286   5 SYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGV 74
PRK14279 PRK14279
molecular chaperone DnaJ;
19-80 4.80e-21

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 94.41  E-value: 4.80e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQ 80
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDE 73
PRK14295 PRK14295
molecular chaperone DnaJ;
19-98 8.32e-21

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 93.76  E-value: 8.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLgiylfdhFGEDGVR 98
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEARSL-------FGNGGFR 84
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 19-83 1.29e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 91.54  E-value: 1.29e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPD--KNPGdiqAAEFFKEINTAHAVLSDPTKKRIYDQHGS 83
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDvnKSPG---AEEKFKEINEAYTVLSDPEKRRIYDTYGT 70
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 19-86 2.22e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 92.22  E-value: 2.22e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNK-EPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGI 74
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 19-93 3.75e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 91.73  E-value: 3.75e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGIYL---FDHFG 93
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGnggFGGFS 84
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 16-85 1.38e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 90.15  E-value: 1.38e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537139217  16 TSLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKN--PGdiqAAEFFKEINTAHAVLSDPTKKRIYDQHGSLG 85
Cdd:PRK14276   4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINkePG---AEEKYKEVQEAYETLSDPQKRAAYDQYGAAG 72
PRK14293 PRK14293
molecular chaperone DnaJ;
19-97 1.94e-19

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 89.66  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPD--KNPGdiqAAEFFKEINTAHAVLSDPTKKRIYDQhgslgiylfdhFGEDG 96
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDvnKEPG---AEDRFKEINRAYEVLSDPETRARYDQ-----------FGEAG 71


                 .
gi 537139217  97 V 97
Cdd:PRK14293  72 V 72
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 19-83 4.23e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 88.45  E-value: 4.23e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQ-AAEFFKEINTAHAVLSDPTKKRIYDQHGS 83
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAeAEEKFKEISEAYEVLSDPQKRRQYDQTGT 71
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
16-80 1.67e-18

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 80.15  E-value: 1.67e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 537139217  16 TSLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQ-AAEFFKEINTAHAVLSDPTKKRIYDQ 80
Cdd:COG2214    5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYDR 70
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 19-96 1.97e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 86.42  E-value: 1.97e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQhgslgiylFDHFGEDG 96
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSE-EEGAEEKFKEISEAYAVLSDDEKRQRYDQ--------FGHAGMDG 76
PRK14280 PRK14280
molecular chaperone DnaJ;
19-85 2.85e-18

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 85.93  E-value: 2.85e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPD--KNPGdiqAAEFFKEINTAHAVLSDPTKKRIYDQHGSLG 85
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDinKEEG---ADEKFKEISEAYEVLSDDQKRAQYDQFGHAG 72
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 18-86 1.09e-17

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 84.87  E-value: 1.09e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 537139217  18 LYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNpGDiqaAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG-GD---PEKFKEISRAYEVLSDPEKRKIYDEYGEEGL 94
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 19-83 3.14e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 83.01  E-value: 3.14e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPgDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGS 83
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDRFGT 68
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 19-85 3.46e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 82.92  E-value: 3.46e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAE-FFKEINTAHAVLSDPTKKRIYDQHGSLG 85
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEqKFKEIQEAYEVLSDPQKRAMYDRFGYVG 74
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 19-82 9.69e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 81.19  E-value: 9.69e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFG 69
Bbox_SF cd00021
B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ...
 202-240 3.93e-16

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


Pssm-ID: 380813 [Multi-domain]  Cd Length: 39  Bit Score: 71.86  E-value: 3.93e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 537139217 202 MCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd00021    1 MCQEHDEEKANKYCVTCEVLYCALCKKSGAHPDHEVAPL 39
PRK14288 PRK14288
molecular chaperone DnaJ;
17-86 1.40e-14

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 74.73  E-value: 1.40e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217  17 SLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDIQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PRK14288   4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGL 73
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 19-82 4.98e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 73.12  E-value: 4.98e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDiQAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAP-DAEDKFKEVKEAYDTLSDPQKKAHYDQFG 69
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 19-82 1.99e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 71.52  E-value: 1.99e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPD--KNPGdiqAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14296   7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDlnKSPD---AHDKMVEINEAADVLLDKDKRKQYDQFG 69
Bbox2_MID cd19758
B-box-type 2 zinc finger found in midline (MID) family; The MID family includes MID1 and MID2. ...
 201-240 4.05e-13

B-box-type 2 zinc finger found in midline (MID) family; The MID family includes MID1 and MID2. MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis, and functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and 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: 380816  Cd Length: 40  Bit Score: 63.26  E-value: 4.05e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19758    1 LMCSEHEEEKVNMYCLTDDQLICSLCKLVGKHKDHEVAAL 40
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 19-82 9.82e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 66.19  E-value: 9.82e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDK-NPGDiqAAEFFKEINTAHAVLSDPTKKRIYDQHG 82
Cdd:PRK14300   6 YQILGVSKTASQADLKKAYLKLAKQYHPDTtDAKD--AEKKFKEINAAYDVLKDEQKRAAYDRFG 68
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
 202-240 1.24e-11

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: 58.96  E-value: 1.24e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 537139217 202 MCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19756    1 LCPEHPEEPLKLFCETCQELVCVLCLLSGEHRGHKVVPL 39
Bbox2_TRIM36_C-I cd19778
B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 201-245 1.72e-11

B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation through interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and 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: 380836  Cd Length: 45  Bit Score: 58.70  E-value: 1.72e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYK 245
Cdd:cd19778    1 LMCPEHEMEKVNMYCEACRRPVCHLCKLGGSHANHRVTSMSSAYK 45
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
19-72 2.49e-10

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 56.34  E-value: 2.49e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPDK-----NPGDIQAA-EFFKEINTAHAVLSDP 72
Cdd:COG1076    7 FELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLAlQKAAAINEAYETLKDP 66
PRK10266 PRK10266
curved DNA-binding protein;
19-80 1.96e-09

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 58.68  E-value: 1.96e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537139217  19 YAVLGIKRGAQPEEIKKAYRKLALQYHPD--KNPgdiQAAEFFKEINTAHAVLSDPTKKRIYDQ 80
Cdd:PRK10266   7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDvsKEP---DAEARFKEVAEAWEVLSDEQRRAEYDQ 67
Bbox2_MID2_C-I cd19823
B-box-type 2 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 201-240 4.22e-09

B-box-type 2 zinc finger found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase that is highly related to MID1 that associate with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. It heterodimerizes in vitro with its paralog MID1. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and 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: 380881  Cd Length: 40  Bit Score: 51.90  E-value: 4.22e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19823    1 LTCLEHENEKVNMYCVVDDQLICALCKLVGRHRDHQVASL 40
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 18-79 1.38e-08

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 56.58  E-value: 1.38e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 537139217  18 LYAVLGIKR---GAQPEEIKKAYRKLALQYHPDKNP--GDIQAAEFFKEINTAHAVLSDPTKKRIYD 79
Cdd:COG5269   45 LYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYD 111
Bbox2_MID1_C-I cd19822
B-box-type 2 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed ...
 201-240 9.74e-08

B-box-type 2 zinc finger found in midline-1 (MID1) and similar proteins; MID1, also termed midin, or midline 1 RING finger protein, or putative transcription factor XPRF, or RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRI18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. It heterodimerizes in vitro with its paralog MID2. MID1 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380880  Cd Length: 47  Bit Score: 48.11  E-value: 9.74e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 537139217 201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19822    6 LMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAAL 45
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 9-86 1.06e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.41  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537139217    9 RQLSKTGTSLYAVLGIKRGAQPEEIKKAYRKLALQYHPDKNPGDiQAAEFFKEINTAHAVLSDPTKKRIYDQHGSLGI 86
Cdd:PTZ00341  566 PTIEIPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGN-EGFHKFKKINEAYQILGDIDKKKMYNKFGYDGI 642
zf-B_box pfam00643
B-box zinc finger;
199-240 3.12e-07

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 46.70  E-value: 3.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 537139217  199 QHLMCEEHEDEKINIYCLSCEVPTCSLCKVfGAHKDCEVAPL 240
Cdd:pfam00643   2 KERLCPEHEEEPLTLYCNDCQELLCEECSV-GEHRGHTVVPL 42
djlA PRK09430
co-chaperone DjlA;
15-48 4.86e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.97  E-value: 4.86e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 537139217  15 GTSL---YAVLGIKRGAQPEEIKKAYRKLALQYHPDK 48
Cdd:PRK09430 196 GPTLedaYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
Bbox2_TRIM67_C-I cd19827
B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 203-245 1.11e-06

B-box-type 2 zinc finger found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380885  Cd Length: 45  Bit Score: 45.36  E-value: 1.11e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 537139217 203 CEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYK 245
Cdd:cd19827    3 CAEHELENYSMYCASCRTPVCYQCLEEGKHAKHEVKALGAMWK 45
Bbox2_TRIM9-like cd19764
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and ...
 202-240 1.26e-06

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM9, TRIM67 and similar proteins; This family includes a group of tripartite motif-containing proteins including TRIM9 and TRIM67, both of which belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and 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. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. It plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also termed TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis.


Pssm-ID: 380822  Cd Length: 39  Bit Score: 44.69  E-value: 1.26e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 537139217 202 MCEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPL 240
Cdd:cd19764    1 TCSEHPDEALSMYCLSCKVPVCYLCLEDGRHSNHDVQAL 39
BBOX smart00336
B-Box-type zinc finger;
201-240 6.88e-06

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 42.71  E-value: 6.88e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 537139217   201 LMCEEHEDEKINIYCLSCEVPTCSLCKVFgAHKDCEVAPL 240
Cdd:smart00336   4 PKCDSHGDEPAEFFCEECGALLCRTCDEA-EHRGHTVVLL 42
Bbox2_TRIM46_C-I cd19786
B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 201-245 1.21e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and 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: 380844 [Multi-domain]  Cd Length: 46  Bit Score: 42.21  E-value: 1.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 537139217 201 LMCEEHeDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYK 245
Cdd:cd19786    3 LMCPEH-KEEVTHYCKTCQRLVCQLCRVRRTHAGHKITPVLSAYQ 46
Bbox2_TRIM9_C-I cd19826
B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 203-245 2.92e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9 (the human ortholog of rat Spring), also termed RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducer repeat-containing protein (beta-TCP) through its N-terminal degron motif (DSGXXS) depending on the phosphorylation status, and thus negatively regulate nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytosis soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, the fibronectin type III domain and the SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380884  Cd Length: 49  Bit Score: 41.24  E-value: 2.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 537139217 203 CEEHEDEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYK 245
Cdd:cd19826    7 CTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWK 49
Bbox2_TRIM14 cd19768
B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar ...
 203-238 4.43e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins; TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380826 [Multi-domain]  Cd Length: 44  Bit Score: 40.48  E-value: 4.43e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 537139217 203 CEEHEDEKINIYCLSCEVPTCSLCKVFGAHK--DCEVA 238
Cdd:cd19768    3 CPEHKDRPLELFCKTCKRCVCALCPILGQHRghDVRLI 40
Bbox2_TRIM71_C-VII cd19796
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ...
 203-226 2.13e-03

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: 36.13  E-value: 2.13e-03
                         10        20
                 ....*....|....*....|....
gi 537139217 203 CEEHEDEKINIYCLSCEVPTCSLC 226
Cdd:cd19796    4 CEIHEHEVLRLYCDTCSVPICREC 27
Bbox2_BRAT-like cd19798
B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ...
 198-233 2.31e-03

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


Pssm-ID: 380856  Cd Length: 44  Bit Score: 35.74  E-value: 2.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 537139217 198 EQHLMCEEHEDEKINIYCLSCEVPTCSLCKVF----GAHK 233
Cdd:cd19798    1 EKPVFCPKHPNEVLKFFCKTCNIPICKDCTLLdhnkGLHD 40
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 247-350 3.59e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 37.24  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217   247 QKSELSDGIAMLVAGNDRVQAVITQMEEVCQTIEDNSRRQKQLLNQRFETLCAVLEERKGELLQALAREQEEKLQRVRGL 326
Cdd:smart00502   1 QREALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQ 80

                           90       100
                   ....*....|....*....|....
gi 537139217   327 IrqygDHLEVSSKLVESAIQSMEE 350
Cdd:smart00502  81 L----ESLTQKQEKLSHAINFTEE 100
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 265-359 4.90e-03

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: 36.75  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537139217 265 VQAVITQMEEVCQTIEDNSRRQKQLLNQRFETLCAVLEERKGELLQALAR---EQEEKLQRVRGLIRQYGDHLEVSSKLV 341
Cdd:cd20482   19 LRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESiynAKQLSLNEQQQKLQETIEKIQQGCEFT 98

                         90
                 ....*....|....*...
gi 537139217 342 ESAIQSMEEPQMALYLQQ 359
Cdd:cd20482   99 ERLLKHGSETEVLLFKKL 116
 
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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