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Conserved domains on  [gi|255714913|ref|XP_002553738|]
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KLTH0E05896p [Lachancea thermotolerans CBS 6340]

Protein Classification

RING-Ubox_PRP19 and Prp19 domain-containing protein( domain architecture ID 11616144)

RING-Ubox_PRP19 and Prp19 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
75-138 8.29e-31

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


:

Pssm-ID: 400774  Cd Length: 65  Bit Score: 113.76  E-value: 8.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255714913   75 YSIPNLLSALQDEWDAVMLENFQLRQQIEASKKELSTALYRCDAAMNVAARATMEADKLKQELN 138
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALA 64
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
1-53 4.13e-22

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


:

Pssm-ID: 438318  Cd Length: 54  Bit Score: 89.16  E-value: 4.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255714913   1 MFCAISGKPPKTASFSPSSKCVFEKSLIEAYVAENGIDPISKEPLQIDQLVEI 53
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEI 53
 
Name Accession Description Interval E-value
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
75-138 8.29e-31

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


Pssm-ID: 400774  Cd Length: 65  Bit Score: 113.76  E-value: 8.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255714913   75 YSIPNLLSALQDEWDAVMLENFQLRQQIEASKKELSTALYRCDAAMNVAARATMEADKLKQELN 138
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALA 64
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
1-53 4.13e-22

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 438318  Cd Length: 54  Bit Score: 89.16  E-value: 4.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255714913   1 MFCAISGKPPKTASFSPSSKCVFEKSLIEAYVAENGIDPISKEPLQIDQLVEI 53
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEI 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
1-53 3.67e-09

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: 53.01  E-value: 3.67e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 255714913     1 MFCAISGKPPKTASFSPSSKcVFEKSLIEAYVAENGIDPISKEPLQIDQLVEI 53
Cdd:smart00504   2 FLCPISLEVMKDPVILPSGQ-TYERSAIEKWLLSHGTDPVTGQPLTHEDLIPN 53
 
Name Accession Description Interval E-value
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
75-138 8.29e-31

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


Pssm-ID: 400774  Cd Length: 65  Bit Score: 113.76  E-value: 8.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255714913   75 YSIPNLLSALQDEWDAVMLENFQLRQQIEASKKELSTALYRCDAAMNVAARATMEADKLKQELN 138
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALA 64
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
1-53 4.13e-22

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 438318  Cd Length: 54  Bit Score: 89.16  E-value: 4.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255714913   1 MFCAISGKPPKTASFSPSSKCVFEKSLIEAYVAENGIDPISKEPLQIDQLVEI 53
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEI 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
1-53 3.67e-09

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: 53.01  E-value: 3.67e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 255714913     1 MFCAISGKPPKTASFSPSSKcVFEKSLIEAYVAENGIDPISKEPLQIDQLVEI 53
Cdd:smart00504   2 FLCPISLEVMKDPVILPSGQ-TYERSAIEKWLLSHGTDPVTGQPLTHEDLIPN 53
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
3-45 8.07e-05

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: 39.84  E-value: 8.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255714913   3 CAISGKPPKTASFSPSSKcVFEKSLIEAYVAENGIDPISKEPL 45
Cdd:cd16453    3 CPISGELMKDPVITPSGI-TYDRSAIERWLLSDNTDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
23-51 1.59e-03

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: 37.17  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 255714913  23 FEKSLIEAYVAENG-IDPISKEPLQIDQLV 51
Cdd:cd16654   26 YERKDIEEHLQRVGhFDPITREPLTQDQLI 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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