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Conserved domains on  [gi|257698067|emb|CBC86743|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

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 ...
 291-343 1.90e-30

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: 113.43  E-value: 1.90e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSL 343
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 410-449 1.71e-09

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: 53.61  E-value: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 257698067  410 NPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLS 449
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 406-541 1.13e-08

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  406 LARENPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNlsIDEVNKKLISNE---GAIPNIIEILENGNREARENS 482
Cdd:PLN03200 1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRRHEsafGAVNQLVAVLRLGSRSARYSA 1252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 257698067  483 AAALFSLSMLDENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLSLNSANKGRAI 541
Cdd:PLN03200 1253 ARALQELFSAEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAI 1311
MLKL_NTD super family cl41936
N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; ...
 52-154 3.52e-03

N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; MLKL is a pseudokinase that does not have protein kinase activity and plays a key role in tumor necrosis factor (TNF)-induced necroptosis, a programmed cell death process. The model corresponds to the MLKL N-terminal region that reveals a four-helix bundle with an additional helix at the top which is likely key for MLKL function. The N-terminal domain binds directly to phospholipids and induces membrane permeabilization.


The actual alignment was detected with superfamily member cd21037:

Pssm-ID: 455281 [Multi-domain]  Cd Length: 138  Bit Score: 38.11  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  52 GLVSDIVSIVEfldqingYRRTQQKECFNLVRRLKILIPFLDEIR----GFESPSCKHFLNRLRKVFLAAKKLLETCSNG 127
Cdd:cd21037    5 GLALEILEAVE-------TVKSNKEACRRLAERVAELLLALEELLegkeEDLSPELREALEELERTLEEIKEFVEKISKR 77

                         90       100
                 ....*....|....*....|....*..
gi 257698067 128 SKIYMALDGETMMTRFHSIYEKLNRVL 154
Cdd:cd21037   78 SRLKRFLKAKSIAEKLEELNERLDDAL 104
 
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 ...
 291-343 1.90e-30

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: 113.43  E-value: 1.90e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSL 343
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 293-356 2.24e-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: 105.01  E-value: 2.24e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257698067   293 EFLCPITLEIMLDPVIIATGQTYEKESIQKWFDaGHKTCPKTRQELDHLSLAPNFALKNLIMQW 356
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 ...
 291-360 2.63e-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: 85.06  E-value: 2.63e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSLAPNFALKNLIMQWCEKN 360
Cdd:pfam04564   2 PDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 410-449 1.71e-09

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: 53.61  E-value: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 257698067  410 NPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLS 449
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 406-541 1.13e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  406 LARENPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNlsIDEVNKKLISNE---GAIPNIIEILENGNREARENS 482
Cdd:PLN03200 1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRRHEsafGAVNQLVAVLRLGSRSARYSA 1252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 257698067  483 AAALFSLSMLDENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLSLNSANKGRAI 541
Cdd:PLN03200 1253 ARALQELFSAEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAI 1311
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 410-449 2.31e-06

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: 44.73  E-value: 2.31e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 257698067   410 NPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLS 449
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
417-530 8.03e-06

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.78  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 417 IANAGAIPLLVQLLSYPDSGIQENAVTTLlnlsidevnkKLISNEGAIPNIIEILENGNREARENSAAALfslsmldenk 496
Cdd:COG1413   12 LGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEAL---------- 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 257698067 497 VTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNL 530
Cdd:COG1413   72 GRIGDPEAVPALIAALKDEDPEVRRAAAEALGRL 105
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 493-531 2.67e-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: 41.67  E-value: 2.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 257698067  493 DENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLS 531
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 493-531 4.17e-04

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: 38.18  E-value: 4.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 257698067   493 DENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLS 531
Cdd:smart00185   2 DENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
MLKL_NTD cd21037
N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; ...
 52-154 3.52e-03

N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; MLKL is a pseudokinase that does not have protein kinase activity and plays a key role in tumor necrosis factor (TNF)-induced necroptosis, a programmed cell death process. The model corresponds to the MLKL N-terminal region that reveals a four-helix bundle with an additional helix at the top which is likely key for MLKL function. The N-terminal domain binds directly to phospholipids and induces membrane permeabilization.


Pssm-ID: 411030 [Multi-domain]  Cd Length: 138  Bit Score: 38.11  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  52 GLVSDIVSIVEfldqingYRRTQQKECFNLVRRLKILIPFLDEIR----GFESPSCKHFLNRLRKVFLAAKKLLETCSNG 127
Cdd:cd21037    5 GLALEILEAVE-------TVKSNKEACRRLAERVAELLLALEELLegkeEDLSPELREALEELERTLEEIKEFVEKISKR 77

                         90       100
                 ....*....|....*....|....*..
gi 257698067 128 SKIYMALDGETMMTRFHSIYEKLNRVL 154
Cdd:cd21037   78 SRLKRFLKAKSIAEKLEELNERLDDAL 104
 
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 ...
 291-343 1.90e-30

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: 113.43  E-value: 1.90e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSL 343
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 293-356 2.24e-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: 105.01  E-value: 2.24e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257698067   293 EFLCPITLEIMLDPVIIATGQTYEKESIQKWFDaGHKTCPKTRQELDHLSLAPNFALKNLIMQW 356
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 291-346 7.17e-21

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: 86.02  E-value: 7.17e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAgHKTCPKTRQELDHLSLAPN 346
Cdd:cd16655    1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDLVPN 55
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 291-360 2.63e-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: 85.06  E-value: 2.63e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSLAPNFALKNLIMQWCEKN 360
Cdd:pfam04564   2 PDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 294-338 4.20e-15

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: 69.51  E-value: 4.20e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 257698067 294 FLCPITLEIMLDPVIIATGQTYEKESIQKWFDAgHKTCPKTRQEL 338
Cdd:cd16453    1 FLCPISGELMKDPVITPSGITYDRSAIERWLLS-DNTDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 291-360 4.09e-13

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: 64.52  E-value: 4.09e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSLAPNFALKNLIMQWCEKN 360
Cdd:cd16654    2 PDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 294-349 1.71e-11

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: 59.42  E-value: 1.71e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257698067 294 FLCPITLEIMLDPVIIATGQTYEKESIQKWFDaGHKTCPKTRQELDHLSLAPNFAL 349
Cdd:cd23149    1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPNREL 55
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 291-356 1.07e-10

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: 57.86  E-value: 1.07e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAgHKTCPKTRQELDHLSLAPNFALKNLIMQW 356
Cdd:cd23150    1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIA-TGNKDETGKKLSIDDVVVFDELYQQIKVY 65
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 410-449 1.71e-09

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: 53.61  E-value: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 257698067  410 NPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLS 449
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 294-353 9.27e-09

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: 52.26  E-value: 9.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257698067 294 FLCPITLEIMLDPVIIAT-GQTYEKESIQKWFDAGHKT--CPKT--RQELDHLSLAPNFALKNLI 353
Cdd:cd16651    1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSRKKKakCPVAgcRNTVSKSDLVPDPELKRRI 65
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 406-541 1.13e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  406 LARENPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNlsIDEVNKKLISNE---GAIPNIIEILENGNREARENS 482
Cdd:PLN03200 1175 LAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLR--ILFSSPELRRHEsafGAVNQLVAVLRLGSRSARYSA 1252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 257698067  483 AAALFSLSMLDENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLSLNSANKGRAI 541
Cdd:PLN03200 1253 ARALQELFSAEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAI 1311
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 415-534 6.30e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 56.26  E-value: 6.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  415 VLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLSIDEVN--KKLISNEGaIPNIIEILENGNREARENSAAALFSLS-M 491
Cdd:PLN03200  398 RKLNHAEAKKVLVGLITMATADVQEELIRALSSLCCGKGGlwEALGGREG-VQLLISLLGLSSEQQQEYAVALLAILTdE 476

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 257698067  492 LDENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLSLNS 534
Cdd:PLN03200  477 VDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHS 519
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 378-489 6.63e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 56.26  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  378 KDEVSLLVEALSSSQLEEQRRSVKQMRLLARENPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNL-SIDEVNKK 456
Cdd:PLN03200  445 REGVQLLISLLGLSSEQQQEYAVALLAILTDEVDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRA 524

                          90       100       110
                  ....*....|....*....|....*....|...
gi 257698067  457 LISNEGAIPNIIEILENGNREARENSAAALFSL 489
Cdd:PLN03200  525 CVESAGAVPALLWLLKNGGPKGQEIAAKTLTKL 557
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 381-547 2.68e-07

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 54.34  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  381 VSLLVEAL--SSSQLEEQRRSVKQMRLLARENPENRVLI-ANAGAIPLLVQLLSYPDSGIQENAVTTLLNLSIDE--VNK 455
Cdd:PLN03200   15 VAQCIEQLraKSSSPQEKELTTARLLELAKTREEARKAIgSHSQAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEEdlRVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  456 KLISneGAIPNIIEILENGNREARENSAAALFSLS---MLDENKVTIGLSNGI-PPLVDLLQHGTLRGK--KDALT-ALF 528
Cdd:PLN03200   95 VLLG--GCIPPLLSLLKSGSAEAQKAAAEAIYAVSsggLSDHVGSKIFSTEGVvPSLWDQLQPGNKQDKvvEGLLTgALR 172

                         170       180
                  ....*....|....*....|
gi 257698067  529 NLSLNSANKGRA-IDAGIVQ 547
Cdd:PLN03200  173 NLCGSTDGFWSAtLEAGGVD 192
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 410-449 2.31e-06

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: 44.73  E-value: 2.31e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 257698067   410 NPENRVLIANAGAIPLLVQLLSYPDSGIQENAVTTLLNLS 449
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
417-530 8.03e-06

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.78  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 417 IANAGAIPLLVQLLSYPDSGIQENAVTTLlnlsidevnkKLISNEGAIPNIIEILENGNREARENSAAALfslsmldenk 496
Cdd:COG1413   12 LGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEAL---------- 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 257698067 497 VTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNL 530
Cdd:COG1413   72 GRIGDPEAVPALIAALKDEDPEVRRAAAEALGRL 105
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 291-325 1.25e-05

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: 43.07  E-value: 1.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFD 325
Cdd:cd16660    1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIK 35
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 493-531 2.67e-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: 41.67  E-value: 2.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 257698067  493 DENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLS 531
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
417-548 2.68e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 47.19  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 417 IANAGAIPLLVQLLSYPDSGIQENAVTTLLNL-SIDEVNKKLISNEGAIPNIIEILENGNREARENSAAALFSLSMLDEN 495
Cdd:COG5064  281 VLDVGIPGRLVELLSHESAKIQTPALRSVGNIvTGSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGNTE 360

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 257698067 496 KV-TIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLSLNSANKGRAI----DAGIVQP 548
Cdd:COG5064  361 QIqAVIDANLIPPLIHLLSSAEYKIKKEACWAISNATSGGLNRPDIIrylvSQGFIKP 418
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 290-346 3.49e-05

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: 41.67  E-value: 3.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 257698067 290 LPHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFD--AGHKTCPKTRQELDHLSLAPN 346
Cdd:cd16611    1 LTEELHCPLCLDFFRDPVMLSCGHNFCQSCITGFWElqAEDTTCPECRELCQYRNLTPN 59
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
359-513 8.74e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 45.65  E-value: 8.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 359 KNNFKIPEKEVSPDSQNEQK--DEVSLLVEALSSSQLEEQRRSVKQMR-LLARE-NPENRVLIAnAGAIPLLVQLL-SYP 433
Cdd:COG5064   49 RNLADVSEEAESSFIPMEQQfySELPQLTQQLFSDDIEQQLQAVYKFRkLLSKEtSPPIQPVID-AGVVPRFVEFMdEIQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 434 DSGIQENAVTTLLNLSIDEVNK-KLISNEGAIPNIIEILENGNREARENSAAALFSLSMLDENKVTIGLSNG-IPPLVDL 511
Cdd:COG5064  128 RDMLQFEAAWALTNIASGTTQQtKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGCRDYVLQCGaLEPLLGL 207


                 ..
gi 257698067 512 LQ 513
Cdd:COG5064  208 LL 209
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
 293-336 3.63e-04

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 438160 [Multi-domain]  Cd Length: 52  Bit Score: 38.64  E-value: 3.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 257698067 293 EFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHK-TCPKTRQ 336
Cdd:cd16497    1 EFLCHCCYDLLVNPTTLNCGHSFCRHCLALWWKSSKKtECPECRQ 45
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 493-531 4.17e-04

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: 38.18  E-value: 4.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 257698067   493 DENKVTIGLSNGIPPLVDLLQHGTLRGKKDALTALFNLS 531
Cdd:smart00185   2 DENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
381-489 4.26e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 40.77  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 381 VSLLVEALSSSQLEEQRRSVKQ-------------MRLLARENPENRVLIANA-------GAIPLLVQLLSYPDSGIQEN 440
Cdd:COG1413   18 VPALIAALADEDPDVRAAAARAlgrlgdpravpalLEALKDPDPEVRAAAAEAlgrigdpEAVPALIAALKDEDPEVRRA 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 257698067 441 AVTTLLNlsidevnkklISNEGAIPNIIEILENGNREARENSAAALFSL 489
Cdd:COG1413   98 AAEALGR----------LGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 291-356 4.51e-04

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: 39.18  E-value: 4.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067 291 PHEFLCPITLEIMLDPVIIATGQTYEKESIQKwfdagH----KTCPKTRQELDHLSLAPNFALKNLIMQW 356
Cdd:cd16658    5 PDEFLDPLMDTLMTDPVILPSGTIMDRSIILR-----HllnsQTDPFNRQPLTEDMLEPVPELKERIQAW 69
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
 296-338 4.94e-04

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 38.41  E-value: 4.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 257698067 296 CPITLEIMLDPVIIATGQTYEKESIQKWFDaGHKTCPKTRQEL 338
Cdd:cd16561    5 CSICLEDLNDPVKLPCDHVFCEECIRQWLP-GQMSCPLCRTEL 46
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 293-335 6.21e-04

first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.


Pssm-ID: 438500 [Multi-domain]  Cd Length: 48  Bit Score: 37.81  E-value: 6.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 257698067 293 EFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTR 335
Cdd:cd23138    2 ELNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQGKKTCGTCR 44
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 293-353 6.90e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 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: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 38.73  E-value: 6.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257698067 293 EFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHKTCPKTRQELDHLSLAPNFALKNLI 353
Cdd:cd16596    9 EVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMV 69
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 420-509 1.48e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 42.01  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  420 AGAIPLLVQLLSYPDSGIQENAVTTLLNL-SIDEVNKKLISNEGAIPNIIEILENGNR-EARENSAAALFSLSM-LDENK 496
Cdd:PLN03200  188 AGGVDILVKLLSSGNSDAQANAASLLARLmMAFESSISKVLDAGAVKQLLKLLGQGNEvSVRAEAAGALEALSSqSKEAK 267

                          90
                  ....*....|...
gi 257698067  497 VTIGLSNGIPPLV 509
Cdd:PLN03200  268 QAIADAGGIPALI 280
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
 294-332 1.57e-03

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: 36.85  E-value: 1.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 257698067 294 FLCPITLEIMLDPVIIAT-GQTYEKESIQKWFDAGHKT--CP 332
Cdd:cd16452    1 LKCPITQKRMKDPVRGKHcGHCFDLEAILQYLKRRKKKwkCP 42
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 291-339 3.04e-03

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 36.23  E-value: 3.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 257698067 291 PHEFLCPITLEIMLDPVIIA-TGQTYEKESIQKWFDAGHKTCPKTRQELD 339
Cdd:cd16620    1 PDELKCPICKDLMKDAVLTPcCGNSFCDECIRTALLEEDFTCPTCKEPDV 50
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 289-337 3.10e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV 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 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: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 36.52  E-value: 3.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 257698067 289 ILPHEFLCPITLEIMLDPVIIATGQTYEKESIQKWFDAGHK---TCPKTRQE 337
Cdd:cd16597    1 DLEEELTCSICLELFKDPVTLPCGHNFCGVCIEKTWDSQHGseySCPQCRAT 52
MLKL_NTD cd21037
N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; ...
 52-154 3.52e-03

N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; MLKL is a pseudokinase that does not have protein kinase activity and plays a key role in tumor necrosis factor (TNF)-induced necroptosis, a programmed cell death process. The model corresponds to the MLKL N-terminal region that reveals a four-helix bundle with an additional helix at the top which is likely key for MLKL function. The N-terminal domain binds directly to phospholipids and induces membrane permeabilization.


Pssm-ID: 411030 [Multi-domain]  Cd Length: 138  Bit Score: 38.11  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257698067  52 GLVSDIVSIVEfldqingYRRTQQKECFNLVRRLKILIPFLDEIR----GFESPSCKHFLNRLRKVFLAAKKLLETCSNG 127
Cdd:cd21037    5 GLALEILEAVE-------TVKSNKEACRRLAERVAELLLALEELLegkeEDLSPELREALEELERTLEEIKEFVEKISKR 77

                         90       100
                 ....*....|....*....|....*..
gi 257698067 128 SKIYMALDGETMMTRFHSIYEKLNRVL 154
Cdd:cd21037   78 SRLKRFLKAKSIAEKLEELNERLDDAL 104
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
 293-332 4.44e-03

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: 35.73  E-value: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 257698067  293 EFLCPITLEIMLDPVI-IATGQTYEKESIQKWFDA-GHKTCP 332
Cdd:pfam11789  11 SLTCPLTLQPFVEPVTsKKCNHVFEKDAILEMLKRnPTVKCP 52
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 294-337 4.68e-03

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438321  Cd Length: 52  Bit Score: 35.63  E-value: 4.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 257698067 294 FLCPITLEIMLD---PVIIATGQTYEKESIQKWFDA--GHKTCPKTRQE 337
Cdd:cd16659    3 LVCRITGEVMNEhnpPLALPNGYVYSEKALEEMAEKndGKVVCPRTGES 51
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 290-336 7.22e-03

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 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: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 35.17  E-value: 7.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 257698067 290 LPHEFLCPITLEIMLDPVIIATGQTYEKESI-QKWFDAGHKTCPKTRQ 336
Cdd:cd16608    3 LKDELLCSICLSIYQDPVSLGCEHYFCRQCItEHWSRSEHRDCPECRR 50
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
 296-338 8.65e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 35.04  E-value: 8.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 257698067 296 CPITLEIMLDPVIIATGQTYEKESIQKWFDAG-HKTCPKTRQEL 338
Cdd:cd16568    7 CIICHEYLYEPMVTTCGHTYCYTCLNTWFKSNrSLSCPDCRTKI 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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