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Conserved domains on  [gi|1002238106|ref|XP_015623258|]
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U-box domain-containing protein 11 [Oryza sativa Japonica Group]

Protein Classification

U-box domain-containing protein( domain architecture ID 11616232)

U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0061630|GO:0004842
PubMed:  12646216|10704423
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 263-315 4.11e-29

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


:

Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 109.57  E-value: 4.11e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITL 315
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 381-623 2.63e-11

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 2.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  381 LAKKSTDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNlsIYDQNKELI---VVAGAIVPIIQVLRKGGMEARENA 457
Cdd:PLN03200  1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRrheSAFGAVNQLVAVLRLGSRSARYSA 1252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  458 AAAIfsLSLIDDNKITIGSTPG-AIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRA---VRAGILAPLIQMLQDSS 533
Cdd:PLN03200  1253 ARAL--QELFSAEHIRDSELARqAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILSSDS 1330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  534 RNGAIDEALTILSVLVSHHECKIAIAKAHAIPFLIDLLRSSQARNKENAAAILLALCkkDAENLA-CIGRLGAQIPLTE- 611
Cdd:PLN03200  1331 SLELKEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLL--DDEQLAeLVAAHGAVVPLVGl 1408

                          250       260
                   ....*....|....*....|....*..
gi 1002238106  612 ---------------LSKTGTDRAKRK 623
Cdd:PLN03200  1409 vvgtnyvlheaaisaLIKLGKDRPPCK 1435
 
Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 263-315 4.11e-29

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 109.57  E-value: 4.11e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITL 315
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 265-328 8.97e-27

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 103.08  E-value: 8.97e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002238106  265 DFRCPISLELMRDPVIVSTGQTYERAFIQRWIDcGNRTCPKTQLKLQNITLTPNYVLRSLILQW 328
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 262-334 1.65e-20

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 85.83  E-value: 1.65e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITLTPNYVLRSLILQWCEEKGI 334
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 381-623 2.63e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 2.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  381 LAKKSTDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNlsIYDQNKELI---VVAGAIVPIIQVLRKGGMEARENA 457
Cdd:PLN03200  1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRrheSAFGAVNQLVAVLRLGSRSARYSA 1252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  458 AAAIfsLSLIDDNKITIGSTPG-AIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRA---VRAGILAPLIQMLQDSS 533
Cdd:PLN03200  1253 ARAL--QELFSAEHIRDSELARqAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILSSDS 1330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  534 RNGAIDEALTILSVLVSHHECKIAIAKAHAIPFLIDLLRSSQARNKENAAAILLALCkkDAENLA-CIGRLGAQIPLTE- 611
Cdd:PLN03200  1331 SLELKEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLL--DDEQLAeLVAAHGAVVPLVGl 1408

                          250       260
                   ....*....|....*....|....*..
gi 1002238106  612 ---------------LSKTGTDRAKRK 623
Cdd:PLN03200  1409 vvgtnyvlheaaisaLIKLGKDRPPCK 1435
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 385-424 1.49e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 47.83  E-value: 1.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002238106 385 STDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNLS 424
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 385-424 1.78e-05

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 42.03  E-value: 1.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002238106  385 STDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNLS 424
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
351-506 4.47e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 43.85  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 351 GERVAIETLVRNLSSSSLDERKSAAaeiRSLAKkstdnrilLAESGAISALVKLLSSKDLKTQEHAVTALLNLSiydqnk 430
Cdd:COG1413    13 GDPAAVPALIAALADEDPDVRAAAA---RALGR--------LGDPRAVPALLEALKDPDPEVRAAAAEALGRIG------ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002238106 431 elivVAGAIVPIIQVLRKGGMEARenaAAAIFSLSLIDDnkitigstPGAIEALVELLQSGSPRGRKDAATALFNL 506
Cdd:COG1413    76 ----DPEAVPALIAALKDEDPEVR---RAAAEALGRLGD--------PAAVPALLEALKDPDWEVRRAAARALGRL 136
 
Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 263-315 4.11e-29

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 109.57  E-value: 4.11e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITL 315
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 265-328 8.97e-27

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 103.08  E-value: 8.97e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002238106  265 DFRCPISLELMRDPVIVSTGQTYERAFIQRWIDcGNRTCPKTQLKLQNITLTPNYVLRSLILQW 328
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 262-334 1.65e-20

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 85.83  E-value: 1.65e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITLTPNYVLRSLILQWCEEKGI 334
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 263-318 3.25e-20

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 84.09  E-value: 3.25e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDcGNRTCPKTQLKLQNITLTPN 318
Cdd:cd16655     1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLE-THNTSPMTRLPLSSTDLVPN 55
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 266-310 3.24e-13

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 64.11  E-value: 3.24e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002238106 266 FRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNrTCPKTQLKL 310
Cdd:cd16453     1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDN-TDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 262-331 1.96e-12

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 62.59  E-value: 1.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRTCPKTQLKLQNITLTPNYVLRSLILQWCEE 331
Cdd:cd16654     1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEE 70
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 263-332 2.05e-12

second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 62.48  E-value: 2.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNrTCPKTQLKLQNITLTPNYVLRSLILQWCEEK 332
Cdd:cd23150     1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATG-NKDETGKKLSIDDVVVFDELYQQIKVYNFYR 69
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 381-623 2.63e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 2.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  381 LAKKSTDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNlsIYDQNKELI---VVAGAIVPIIQVLRKGGMEARENA 457
Cdd:PLN03200  1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRrheSAFGAVNQLVAVLRLGSRSARYSA 1252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  458 AAAIfsLSLIDDNKITIGSTPG-AIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRA---VRAGILAPLIQMLQDSS 533
Cdd:PLN03200  1253 ARAL--QELFSAEHIRDSELARqAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILSSDS 1330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  534 RNGAIDEALTILSVLVSHHECKIAIAKAHAIPFLIDLLRSSQARNKENAAAILLALCkkDAENLA-CIGRLGAQIPLTE- 611
Cdd:PLN03200  1331 SLELKEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLL--DDEQLAeLVAAHGAVVPLVGl 1408

                          250       260
                   ....*....|....*....|....*..
gi 1002238106  612 ---------------LSKTGTDRAKRK 623
Cdd:PLN03200  1409 vvgtnyvlheaaisaLIKLGKDRPPCK 1435
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 398-632 1.00e-10

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 65.12  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  398 ISALVKLLSSKDLKTQEHAVTALLNLSiyDQNKE---LIVVAGAIVPIIQVLRKGGMEARENAAAAIFSL-SLIDDNKIT 473
Cdd:PLN03200   448 VQLLISLLGLSSEQQQEYAVALLAILT--DEVDEskwAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRAC 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  474 IgSTPGAIEALVELLQSGSPRGRKDAATALFNLciyqankVRAVRAGILAPLIQMLQD---SSRNGAIDEALTILSVlVS 550
Cdd:PLN03200   526 V-ESAGAVPALLWLLKNGGPKGQEIAAKTLTKL-------VRTADAATISQLTALLLGdlpESKVHVLDVLGHVLSV-AS 596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  551 HHE-CKIAIAKAHAIPFLIDLLRSSQARNKENAAAILLAL--CKKD-AENLACIGRLGaqiPLTELSKTGTDRAKRKATS 626
Cdd:PLN03200   597 LEDlVREGSAANDALRTLIQLLSSSKEETQEKAASVLADIfsSRQDlCESLATDEIIN---PCIKLLTNNTEAVATQSAR 673


                   ....*.
gi 1002238106  627 LLEHLS 632
Cdd:PLN03200   674 ALAALS 679
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 266-321 3.63e-10

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 55.95  E-value: 3.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002238106 266 FRCPISLELMRDPVIVSTGQTYERAFIQRWIDcGNRTCPKTQLKLQNITLTPNYVL 321
Cdd:cd23149     1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPNREL 55
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 355-548 2.80e-09

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 60.50  E-value: 2.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  355 AIETLVRNLSSSSLDERKSAAAEIRSLAKKSTDNRILLAESGAISALVKLLSSKDLKTQEHAVTAL--LNLSIYDQNKEL 432
Cdd:PLN03200   610 ALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSARALaaLSRSIKENRKVS 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  433 IVVAGAIVPIIQVLRKGGMEARENAAAAIfsLSLIDDNKITIGSTPG-AIEALVELLQSGSPRGRKDAATALFNLC---- 507
Cdd:PLN03200   690 YAAEDAIKPLIKLAKSSSIEVAEQAVCAL--ANLLSDPEVAAEALAEdIILPLTRVLREGTLEGKRNAARALAQLLkhfp 767

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1002238106  508 IYQANKVRAVRAGILAPLIQMLQD-SSRNGAIDEALTILSVL 548
Cdd:PLN03200   768 VDDVLKDSVQCRGTVLALVDLLNStDLDSSATSEALEALALL 809
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 364-568 6.91e-09

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 59.35  E-value: 6.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  364 SSSSLDERKSAAAEIRSLAKKSTDNRILLAE-SGAISALVKLLSSKDLKTQEHAVTALLNLSIYDQNKELIVVAGAIVPI 442
Cdd:PLN03200    25 KSSSPQEKELTTARLLELAKTREEARKAIGShSQAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEEDLRVKVLLGGCIPPL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  443 IQVLRKGGMEARENAAAAIFSLSL--IDDN---KI--TIGSTP------------------------------------- 478
Cdd:PLN03200   105 LSLLKSGSAEAQKAAAEAIYAVSSggLSDHvgsKIfsTEGVVPslwdqlqpgnkqdkvveglltgalrnlcgstdgfwsa 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  479 ----GAIEALVELLQSGSPRGRKDAATALFNLC-IYQANKVRAVRAGILAPLIQMLQDSSRNGAIDEALTILSVLVSHH- 552
Cdd:PLN03200   185 tleaGGVDILVKLLSSGNSDAQANAASLLARLMmAFESSISKVLDAGAVKQLLKLLGQGNEVSVRAEAAGALEALSSQSk 264

                          250
                   ....*....|....*.
gi 1002238106  553 ECKIAIAKAHAIPFLI 568
Cdd:PLN03200   265 EAKQAIADAGGIPALI 280
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 266-325 2.60e-08

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 50.72  E-value: 2.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002238106 266 FRCPISLELMRDPVIVST-GQTYERAFIQRWIDC--GNRTCPKTQL--KLQNITLTPNYVLRSLI 325
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSrkKKAKCPVAGCrnTVSKSDLVPDPELKRRI 65
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 385-424 1.49e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 47.83  E-value: 1.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002238106 385 STDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNLS 424
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 397-585 1.28e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 52.03  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  397 AISALVKLLSSKDLKTQEHAVTALLNLSIYDQN-KELIVVAGAIVPIIQVLRKGGMEARENAAAAIFSLSL-IDDNKITI 474
Cdd:PLN03200   610 ALRTLIQLLSSSKEETQEKAASVLADIFSSRQDlCESLATDEIINPCIKLLTNNTEAVATQSARALAALSRsIKENRKVS 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  475 GSTPGAIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRAVRAGILAPLIQMLQDSSRNGAIDEALTILSVLVSHHEC 554
Cdd:PLN03200   690 YAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLLKHFPVD 769

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1002238106  555 KIAIAKAH---AIPFLIDLLRSSQARNKENAAAI 585
Cdd:PLN03200   770 DVLKDSVQcrgTVLALVDLLNSTDLDSSATSEAL 803
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 262-318 1.42e-06

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the 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 C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 45.90  E-value: 1.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIQRWID--CGNRTCPKTQLKLQNITLTPN 318
Cdd:cd16611     1 LTEELHCPLCLDFFRDPVMLSCGHNFCQSCITGFWElqAEDTTCPECRELCQYRNLTPN 59
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 340-631 2.68e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 50.87  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  340 SKNDG---AYLEVGGervaIETLVRNLSSSSLDERKSAAAEIRSLAKKSTDNRILLAESGAISALVKLLSSK-DLKTQEH 415
Cdd:PLN03200   176 GSTDGfwsATLEAGG----VDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGnEVSVRAE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  416 AVTALLNLSIY-DQNKELIVVAGAIVPIIQVL---RKGGMEAR------ENAAAAIFSLSliddnkitiGSTPGAIEALV 485
Cdd:PLN03200   252 AAGALEALSSQsKEAKQAIADAGGIPALINATvapSKEFMQGEfaqalqENAMGALANIC---------GGMSALILYLG 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  486 ELLQSG-SPRGRKDAATAL-FNLCIYQ--ANKVRAVRA----GILAPLI-----QMLQDSsrngaIDEAL------TILS 546
Cdd:PLN03200   323 ELSESPrSPAPIADTLGALaYALMVFDssAESTRAFDPtvieQILVKLLkprdtKLVQER-----IIEALaslygnAYLS 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  547 VLVSHHECKI---------------------------------AIAKAHAIPFLIDLLRSSQARNKENAAAILLALCKKD 593
Cdd:PLN03200   398 RKLNHAEAKKvlvglitmatadvqeeliralsslccgkgglweALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDEV 477

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1002238106  594 AENLACIGRLGAQIPLTELSKTGTDRAKRKATSLLEHL 631
Cdd:PLN03200   478 DESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNL 515
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 371-631 3.49e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 50.49  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  371 RKSAAAEIRSLAKKSTDNRILLAESGAISALVK--LLSSKDL-------KTQEHAVTALLNLS----------------- 424
Cdd:PLN03200   249 RAEAAGALEALSSQSKEAKQAIADAGGIPALINatVAPSKEFmqgefaqALQENAMGALANICggmsalilylgelsesp 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  425 ------------------IYDQNKElivVAGAIVP--IIQVLRKGgMEAREN---------AAAAIFS---LSLIDDNKi 472
Cdd:PLN03200   329 rspapiadtlgalayalmVFDSSAE---STRAFDPtvIEQILVKL-LKPRDTklvqeriieALASLYGnayLSRKLNHA- 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  473 tigstpGAIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRAV--RAGILApLIQMLQDSSRNGAiDEALTILSVLVS 550
Cdd:PLN03200   404 ------EAKKVLVGLITMATADVQEELIRALSSLCCGKGGLWEALggREGVQL-LISLLGLSSEQQQ-EYAVALLAILTD 475

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  551 H-HECKIAIAKAHAIPFLIDLLRSSQARNKENAAAILLALCKKDAENLACIGRLGAQIPLTELSKTGTDRAKRKATSLLE 629
Cdd:PLN03200   476 EvDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLT 555


                   ..
gi 1002238106  630 HL 631
Cdd:PLN03200   556 KL 557
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 262-332 1.08e-05

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 43.80  E-value: 1.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIQRWIdCGNRTCPKTQLKLQNITLTPNYVLRSLILQWCEEK 332
Cdd:cd16658     4 APDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHL-LNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREK 73
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 385-424 1.78e-05

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 42.03  E-value: 1.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002238106  385 STDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNLS 424
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
 266-304 1.83e-05

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 42.24  E-value: 1.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002238106 266 FRCPISLELMRDPVIVST-GQTYERAFIQRWIDCGNRT--CP 304
Cdd:cd16452     1 LKCPITQKRMKDPVRGKHcGHCFDLEAILQYLKRRKKKwkCP 42
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 355-443 4.19e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 47.02  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  355 AIETLVRNLSSSSLDERKSAAAEIRSLAKKSTDNRILLAESGAISALVKLLSSKDLKTQEHAVTALLNLSIYDQNKELIV 434
Cdd:PLN03200  1318 ALENLCKILSSDSSLELKEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVA 1397


                   ....*....
gi 1002238106  435 VAGAIVPII 443
Cdd:PLN03200  1398 AHGAVVPLV 1406
HEAT COG1413
HEAT repeat [General function prediction only];
351-506 4.47e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 43.85  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 351 GERVAIETLVRNLSSSSLDERKSAAaeiRSLAKkstdnrilLAESGAISALVKLLSSKDLKTQEHAVTALLNLSiydqnk 430
Cdd:COG1413    13 GDPAAVPALIAALADEDPDVRAAAA---RALGR--------LGDPRAVPALLEALKDPDPEVRAAAAEALGRIG------ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002238106 431 elivVAGAIVPIIQVLRKGGMEARenaAAAIFSLSLIDDnkitigstPGAIEALVELLQSGSPRGRKDAATALFNL 506
Cdd:COG1413    76 ----DPEAVPALIAALKDEDPEVR---RAAAEALGRLGD--------PAAVPALLEALKDPDWEVRRAAARALGRL 136
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 468-507 4.64e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 40.90  E-value: 4.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002238106 468 DDNKITIGStPGAIEALVELLQSGSPRGRKDAATALFNLC 507
Cdd:pfam00514   2 PENKQAVIE-AGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 452-631 9.97e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.86  E-value: 9.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  452 EARENAAAAIfslsliddnkitiGSTPGAIEALVELLQSGSPRGRKDAATALFNLCIYQANKVRAVRAGILAPLIQMLQD 531
Cdd:PLN03200    44 KTREEARKAI-------------GSHSQAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEEDLRVKVLLGGCIPPLLSLLKS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106  532 SSRNGAIDEALTILSV----LVSHHECKIAIAKAhAIPFLIDLLRSSQARNKENAAAILLAL----CKKDAENLACIGRL 603
Cdd:PLN03200   111 GSAEAQKAAAEAIYAVssggLSDHVGSKIFSTEG-VVPSLWDQLQPGNKQDKVVEGLLTGALrnlcGSTDGFWSATLEAG 189

                          170       180
                   ....*....|....*....|....*...
gi 1002238106  604 GAQIpLTELSKTGTDRAKRKATSLLEHL 631
Cdd:PLN03200   190 GVDI-LVKLLSSGNSDAQANAASLLARL 216
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 263-297 1.58e-04

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


Pssm-ID: 438322  Cd Length: 53  Bit Score: 39.60  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002238106 263 PEDFRCPISLELMRDPVIVSTGQTYERAFIQRWID 297
Cdd:cd16660     1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIK 35
HEAT COG1413
HEAT repeat [General function prediction only];
392-533 2.64e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 41.54  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 392 LAESGAISALVKLLSSKDLKTQEHAVTALlnlsiydqnkELIVVAGAIVPIIQVLRKGGMEARENAAAAifsLSLIDDnk 471
Cdd:COG1413    12 LGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEA---LGRIGD-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002238106 472 itigstPGAIEALVELLQSGSPRGRKDAATALfnlciYQANKVRAVRAgilapLIQMLQDSS 533
Cdd:COG1413    77 ------PEAVPALIAALKDEDPEVRRAAAEAL-----GRLGDPAAVPA-----LLEALKDPD 122
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
 265-304 4.19e-04

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 38.81  E-value: 4.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002238106 265 DFRCPISLELMRDPVIvST--GQTYERAFIQRWIDCGNRT-CP 304
Cdd:pfam11789  11 SLTCPLTLQPFVEPVT-SKkcNHVFEKDAILEMLKRNPTVkCP 52
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 262-321 8.24e-04

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the 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 C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 38.22  E-value: 8.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFI----QRWIDCGNRTCPKTQLKLQNITLTPNYVL 321
Cdd:cd16598     1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSCItdycPISGGHERPVCPLCRKPFKKENIRPNWQL 64
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 262-310 1.11e-03

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 37.33  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002238106 262 IPEDFRCPISLELMRDPVIVSTGQTYERAFIqrwIDCGNRTCPKTQLKL 310
Cdd:cd16644     2 PSVKLYCPLCQRVFKDPVITSCGHTFCRRCA---LTAPGEKCPVDNMKL 47
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 458-589 2.49e-03

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 40.87  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 458 AAAIFSLSLIDDNKITigstPGAIEALVELLQSGSPRGRKDAATALFNlcIYQANKVRAVRAGILAPLIQMLQDSSrnga 537
Cdd:COG5096   110 GFALRTLSLLRVKELL----GNIIDPIKKLLTDPHAYVRKTAALAVAK--LYRLDKDLYHELGLIDILKELVADSD---- 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002238106 538 ideALTILSVLVSHHECKIAIAKAHAIPFLIDLLR---SSQARNKENAAAILLAL 589
Cdd:COG5096   180 ---PIVIANALASLAEIDPELAHGYSLEVILRIPQldlLSLSVSTEWLLLIILEV 231
HEAT COG1413
HEAT repeat [General function prediction only];
436-589 2.50e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 38.46  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 436 AGAIVPIIQVLRKGGMEARENAAAAifsLSLIDDnkitigstPGAIEALVELLQSGSPRGRKDAATALFNLciyqankvR 515
Cdd:COG1413    15 PAAVPALIAALADEDPDVRAAAARA---LGRLGD--------PRAVPALLEALKDPDPEVRAAAAEALGRI--------G 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002238106 516 AVRAgiLAPLIQMLQDSS---RNGAIdEALTilsvlvshheckiAIAKAHAIPFLIDLLRSSQARNKENAAAILLAL 589
Cdd:COG1413    76 DPEA--VPALIAALKDEDpevRRAAA-EALG-------------RLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 266-304 2.51e-03

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the 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 C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 36.31  E-value: 2.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002238106 266 FRCPISLELMRDPVIVSTGQTYERAFIQRWIDCGNRT--CP 304
Cdd:cd16601     2 ASCSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDfpCP 42
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 479-507 3.58e-03

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 35.48  E-value: 3.58e-03
                           10        20
                   ....*....|....*....|....*....
gi 1002238106  479 GAIEALVELLQSGSPRGRKDAATALFNLC 507
Cdd:smart00185  12 GGLPALVELLKSEDEEVVKEAAWALSNLS 40
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 268-304 4.41e-03

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


Pssm-ID: 438111 [Multi-domain]  Cd Length: 42  Bit Score: 35.51  E-value: 4.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002238106 268 CPISLELMRD---PVIVSTGQTYERAFIQRWIDCGNRTCP 304
Cdd:cd00162     1 CPICREEMNDrrpVVLLSCGHTFSRSAIARWLEGSKQKCP 40
HEAT COG1413
HEAT repeat [General function prediction only];
458-594 6.42e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 37.30  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 458 AAAIFSLSLIDDnkitigstPGAIEALVELLQSGSPRGRKDAATALFNLciyqankvRAVRAgiLAPLIQMLQDSS---R 534
Cdd:COG1413     3 RAAARALGRLGD--------PAAVPALIAALADEDPDVRAAAARALGRL--------GDPRA--VPALLEALKDPDpevR 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238106 535 NGAIdEALTilsvlvshheckiAIAKAHAIPFLIDLLRSSQARNKENAAAILLALCKKDA 594
Cdd:COG1413    65 AAAA-EALG-------------RIGDPEAVPALIAALKDEDPEVRRAAAEALGRLGDPAA 110
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 264-305 7.43e-03

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the 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 C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 35.36  E-value: 7.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002238106 264 EDFRCPISLELMRDPVIVSTGQTYERAFIQR-WIDCGNR-TCPK 305
Cdd:cd16594     4 EELTCPICLDYFTDPVTLDCGHSFCRACIARcWEEPETSaSCPQ 47
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 264-309 9.56e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the 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 C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 35.04  E-value: 9.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002238106 264 EDFRCPISLELMRDPVIVSTGQTYERAFIQR-WIDCGNRT--CPKTQLK 309
Cdd:cd16609     2 EELTCSICLGLYQDPVTLPCQHSFCRACIEDhWRQKDEGSfsCPECRAP 50
 
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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