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Conserved domains on  [gi|894216101|ref|NP_001297675|]
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ubiquitin-like protein 5 isoform 1 [Mus musculus]

Protein Classification

Ubl5/Hub1 family ubiquitin-like protein( domain architecture ID 10110356)

Ubl5/Hub1 family ubiquitin-like protein similar to Saccharomyces cerevisiae Hub1 that plays a role in splice-site usage and alternative splicing

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1-111 1.17e-41

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


:

Pssm-ID: 340489  Cd Length: 71  Bit Score: 131.67  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216101   1 MIEVVCNDRLGKKVRVKCNTDDTIGDLKKLIAAQTGTRWNKIVLKKWYTIFKDHVSLGDCilflkfmkeamvdvelqdpa 80
Cdd:cd01791    1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDY-------------------- 60

                         90       100       110
                 ....*....|....*....|....*....|.
gi 894216101  81 vsrwkvvispskflntcpsdEIHDGMNLELY 111
Cdd:cd01791   61 --------------------EIHDGMNLELY 71
 
Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1-111 1.17e-41

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


Pssm-ID: 340489  Cd Length: 71  Bit Score: 131.67  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216101   1 MIEVVCNDRLGKKVRVKCNTDDTIGDLKKLIAAQTGTRWNKIVLKKWYTIFKDHVSLGDCilflkfmkeamvdvelqdpa 80
Cdd:cd01791    1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDY-------------------- 60

                         90       100       110
                 ....*....|....*....|....*....|.
gi 894216101  81 vsrwkvvispskflntcpsdEIHDGMNLELY 111
Cdd:cd01791   61 --------------------EIHDGMNLELY 71
 
Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1-111 1.17e-41

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


Pssm-ID: 340489  Cd Length: 71  Bit Score: 131.67  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216101   1 MIEVVCNDRLGKKVRVKCNTDDTIGDLKKLIAAQTGTRWNKIVLKKWYTIFKDHVSLGDCilflkfmkeamvdvelqdpa 80
Cdd:cd01791    1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDY-------------------- 60

                         90       100       110
                 ....*....|....*....|....*....|.
gi 894216101  81 vsrwkvvispskflntcpsdEIHDGMNLELY 111
Cdd:cd01791   61 --------------------EIHDGMNLELY 71
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 4-60 6.17e-06

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 40.66  E-value: 6.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 894216101   4 VVCNDRLGKKVRVKCNTDDTIGDLKKLIAAQTGTRWNKIVLKKWYTIFKDHVSLGDC 60
Cdd:cd17039    1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDY 57
 
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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