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Conserved domains on  [gi|186910241|ref|NP_001119552|]
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ubiquitin-fold modifier 1 [Rattus norvegicus]

Protein Classification

ubiquitin-fold modifier 1( domain architecture ID 10109924)

ubiquitin fold modifier 1 (UFM1) can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl_UFM1 cd01766
ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ...
4-78 1.77e-52

ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ubiquitin-like protein family with similar ubiquitin beta-grasp folds and mechanism of ligation to other proteins. UFM1 is present in nearly all eukaryotic organisms except fungi. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The UNF1 cascade has been implicated in endoplasmic reticulum functions, cell cycle control and cell differentiation. The involvement of the UFM1 cascade in diseases is diverse; reports include its involvement in ischemic heart diseases, diabetes, gastric lesions, schizophrenia, hip dysplasia and cancer.


:

Pssm-ID: 340465  Cd Length: 75  Bit Score: 157.99  E-value: 1.77e-52
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186910241  4 VSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 78
Cdd:cd01766   1 VTFKITLTSDPKLPFKVLSVPEEAPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 75
 
Name Accession Description Interval E-value
Ubl_UFM1 cd01766
ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ...
4-78 1.77e-52

ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ubiquitin-like protein family with similar ubiquitin beta-grasp folds and mechanism of ligation to other proteins. UFM1 is present in nearly all eukaryotic organisms except fungi. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The UNF1 cascade has been implicated in endoplasmic reticulum functions, cell cycle control and cell differentiation. The involvement of the UFM1 cascade in diseases is diverse; reports include its involvement in ischemic heart diseases, diabetes, gastric lesions, schizophrenia, hip dysplasia and cancer.


Pssm-ID: 340465  Cd Length: 75  Bit Score: 157.99  E-value: 1.77e-52
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186910241  4 VSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 78
Cdd:cd01766   1 VTFKITLTSDPKLPFKVLSVPEEAPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 75
Ufm1 pfam03671
Ubiquitin fold modifier 1 protein; This is a family of short ubiquitin-like proteins, that is ...
3-77 2.22e-47

Ubiquitin fold modifier 1 protein; This is a family of short ubiquitin-like proteins, that is like neither type-1 or type-2. It is a ubiquitin-fold modifier 1 (Ufm1) that is synthesized in a precursor form of 85 amino-acid residues. In humans the enzyme for Ufm1 is Uba5 and the conjugating enzyme is Ufc1. Prior to activation by Uba5 the extra two amino acids at the C-terminal region of the human pro-Ufm1 protein are removed to expose Gly whose residue is necessary for conjugation to target molecule(s). The mature Ufm1 is conjugated to yet unidentified endogenous proteins,. While Ubiquitin and many Ubls possess the conserved C-terminal di-glycine that is adenylated by each specific E1 or E1-like enzyme, respectively, in an ATP-dependent manner, Ufm1(1-83) possesses a single glycine at its C-terminus, which is followed by a Ser-Cys dipeptide in the precursor form of Ufm1. The C-terminally processed Ufm1(1-83) is specifically activated by Uba5, an E1-like enzyme, and then transferred to its cognate Ufc1, an E2-like enzyme.


Pssm-ID: 397643  Cd Length: 75  Bit Score: 144.88  E-value: 2.22e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186910241   3 KVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLI 77
Cdd:pfam03671  1 KVTFKITLTSDPKLPFRVISVPEAAPFTAVLKFAAEEFKVPPATSAIITNDGIGINPAQTAGNVFLKHGSELRLI 75
 
Name Accession Description Interval E-value
Ubl_UFM1 cd01766
ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ...
4-78 1.77e-52

ubiquitin-like (Ubl) domain found in ubiquitin fold modifier 1 (UFM1); UFM1 belongs to the ubiquitin-like protein family with similar ubiquitin beta-grasp folds and mechanism of ligation to other proteins. UFM1 is present in nearly all eukaryotic organisms except fungi. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The UNF1 cascade has been implicated in endoplasmic reticulum functions, cell cycle control and cell differentiation. The involvement of the UFM1 cascade in diseases is diverse; reports include its involvement in ischemic heart diseases, diabetes, gastric lesions, schizophrenia, hip dysplasia and cancer.


Pssm-ID: 340465  Cd Length: 75  Bit Score: 157.99  E-value: 1.77e-52
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186910241  4 VSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 78
Cdd:cd01766   1 VTFKITLTSDPKLPFKVLSVPEEAPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIP 75
Ufm1 pfam03671
Ubiquitin fold modifier 1 protein; This is a family of short ubiquitin-like proteins, that is ...
3-77 2.22e-47

Ubiquitin fold modifier 1 protein; This is a family of short ubiquitin-like proteins, that is like neither type-1 or type-2. It is a ubiquitin-fold modifier 1 (Ufm1) that is synthesized in a precursor form of 85 amino-acid residues. In humans the enzyme for Ufm1 is Uba5 and the conjugating enzyme is Ufc1. Prior to activation by Uba5 the extra two amino acids at the C-terminal region of the human pro-Ufm1 protein are removed to expose Gly whose residue is necessary for conjugation to target molecule(s). The mature Ufm1 is conjugated to yet unidentified endogenous proteins,. While Ubiquitin and many Ubls possess the conserved C-terminal di-glycine that is adenylated by each specific E1 or E1-like enzyme, respectively, in an ATP-dependent manner, Ufm1(1-83) possesses a single glycine at its C-terminus, which is followed by a Ser-Cys dipeptide in the precursor form of Ufm1. The C-terminally processed Ufm1(1-83) is specifically activated by Uba5, an E1-like enzyme, and then transferred to its cognate Ufc1, an E2-like enzyme.


Pssm-ID: 397643  Cd Length: 75  Bit Score: 144.88  E-value: 2.22e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186910241   3 KVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLI 77
Cdd:pfam03671  1 KVTFKITLTSDPKLPFRVISVPEAAPFTAVLKFAAEEFKVPPATSAIITNDGIGINPAQTAGNVFLKHGSELRLI 75
 
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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