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Conserved domains on  [gi|22137475|gb|AAH24507|]
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Ubiquitin-like 3 [Mus musculus]

Protein Classification

ubiquitin family protein( domain architecture ID 13018376)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_UBL3 cd17048
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ...
 10-91 2.15e-63

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins.


:

Pssm-ID: 340568  Cd Length: 82  Bit Score: 187.20  E-value: 2.15e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475  10 INLRLILVSGKTKEFLFSPNDSASDIAKHVYDNWPMDWEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHLV 89
Cdd:cd17048   1 INLRLILVSGKTKEFLFSPNDSAADIAQHVFDNWPEDWEEEQVSSANILRLIYQGRFLHGNVTLGALQLPLGKTTVMHLV 80


                ..
gi 22137475  90 AR 91
Cdd:cd17048  81 AR 82
 
Name Accession Description Interval E-value
Ubl_UBL3 cd17048
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ...
 10-91 2.15e-63

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins.


Pssm-ID: 340568  Cd Length: 82  Bit Score: 187.20  E-value: 2.15e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475  10 INLRLILVSGKTKEFLFSPNDSASDIAKHVYDNWPMDWEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHLV 89
Cdd:cd17048   1 INLRLILVSGKTKEFLFSPNDSAADIAQHVFDNWPEDWEEEQVSSANILRLIYQGRFLHGNVTLGALQLPLGKTTVMHLV 80


                ..
gi 22137475  90 AR 91
Cdd:cd17048  81 AR 82
Rad60-SLD_2 pfam13881
Ubiquitin-2 like Rad60 SUMO-like;
8-114 1.44e-50

Ubiquitin-2 like Rad60 SUMO-like;


Pssm-ID: 372780  Cd Length: 111  Bit Score: 155.54  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475     8 DMINLRLILVSGK-TKEFLFSPNDSASDIAKHVYDNWPMDWEEeQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKT--- 83
Cdd:pfam13881   1 DQIELKFRLVDGSdIGPFVFSPATTVADLKEKVIAQWPKDKEN-GPKTVNDVKLINAGKILENNKTLGECRLPVGETpgg 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 22137475    84 -TVMHLVARETLPEPNSQGQRNREKTGESNCC 114
Cdd:pfam13881  80 vTTMHVVVRPNLPEPNSEKKANKPKQNGCGCC 111
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 10-88 5.24e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 36.08  E-value: 5.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22137475     10 INLRLILVSGKTKEFLFSPNDSASDIAKHVydnwpmdwEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHL 88
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKI--------AELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVL 71
 
Name Accession Description Interval E-value
Ubl_UBL3 cd17048
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; ...
 10-91 2.15e-63

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 3 (UBL3) and similar proteins; UBL3, also termed membrane-anchored ubiquitin-fold protein (MUB), or protein HCG-1, belongs to a newly described MUB protein family with structural homology with ubiquitin. MUB proteins have a beta-grasp ubiquitin-like (Ubl) domain with longer N- and C-termini and extended loops. The Ubl domain contains a C-terminal CAAX-box, a canonical motif for protein prenylation, which is modified through protein lipidation with a hydrophobic membrane anchor. The lipidation and membrane localization inhibit attachment of MUBs to target proteins.


Pssm-ID: 340568  Cd Length: 82  Bit Score: 187.20  E-value: 2.15e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475  10 INLRLILVSGKTKEFLFSPNDSASDIAKHVYDNWPMDWEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHLV 89
Cdd:cd17048   1 INLRLILVSGKTKEFLFSPNDSAADIAQHVFDNWPEDWEEEQVSSANILRLIYQGRFLHGNVTLGALQLPLGKTTVMHLV 80


                ..
gi 22137475  90 AR 91
Cdd:cd17048  81 AR 82
Rad60-SLD_2 pfam13881
Ubiquitin-2 like Rad60 SUMO-like;
8-114 1.44e-50

Ubiquitin-2 like Rad60 SUMO-like;


Pssm-ID: 372780  Cd Length: 111  Bit Score: 155.54  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475     8 DMINLRLILVSGK-TKEFLFSPNDSASDIAKHVYDNWPMDWEEeQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKT--- 83
Cdd:pfam13881   1 DQIELKFRLVDGSdIGPFVFSPATTVADLKEKVIAQWPKDKEN-GPKTVNDVKLINAGKILENNKTLGECRLPVGETpgg 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 22137475    84 -TVMHLVARETLPEPNSQGQRNREKTGESNCC 114
Cdd:pfam13881  80 vTTMHVVVRPNLPEPNSEKKANKPKQNGCGCC 111
Ubl_MUBs_plant cd01814
ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); ...
 9-91 2.56e-09

ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); The plant MUBs belong to a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. They may serve as docking site to facilitate the association of specific E2s to the plasma membrane. MUBs contain a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold.


Pssm-ID: 340512  Cd Length: 89  Bit Score: 50.07  E-value: 2.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475   9 MINLRLILVSG-KTKEFLFSPNDSASDIAKHVYDNWPMDwEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPF----GKT 83
Cdd:cd01814   1 LIEIKFRLTDGsDIGPFRYSSATTVATLKEKVIAEWPKD-KENGPKSINDVKLIYAGKVLENGKTLADSRTPGkvppGGV 79


                ....*...
gi 22137475  84 TVMHLVAR 91
Cdd:cd01814  80 ITMHVVVR 87
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 12-89 1.33e-05

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: 39.89  E-value: 1.33e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22137475  12 LRLILVSGKTKEFLFSPNDSASDIAKHVYDNWPMDWEEeqvsspniLRLIYQGRFLHGNVTLGALKLPFGktTVMHLV 89
Cdd:cd17039   1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQ--------QRLIYNGKELKDDKTLSDYGIKDG--STIHLV 68
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 12-88 1.38e-04

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 37.54  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22137475    12 LRLILVSGKTKEFLFSPNDSASDIAKHVydnwpmdwEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHL 88
Cdd:pfam00240   1 ITVKTLDGKKITLEVDPTDTVLELKEKI--------AEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVL 69
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 10-88 5.24e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 36.08  E-value: 5.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22137475     10 INLRLILVSGKTKEFLFSPNDSASDIAKHVydnwpmdwEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHL 88
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKI--------AELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVL 71
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 12-81 1.36e-03

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 34.61  E-value: 1.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137475  12 LRLILVSGKTKEFLFSPNDSASDIAKHVYdnwpmdweEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFG 81
Cdd:cd00196   1 VKVETPSLKKIVVAVPPSTTLRQVLEKVA--------KRIGLPPDVIRLLFNGQVLDDLMTAKQVGLEPG 62
 
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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