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Conserved domains on  [gi|655845775|ref|XP_008262416|]
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ubiquitin-fold modifier-conjugating enzyme 1 [Oryctolagus cuniculus]

Protein Classification

ubiquitin-fold modifier-conjugating enzyme 1( domain architecture ID 19033447)

ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) is an E1-like enzyme which specifically catalyzes the second step in ufmylation

CATH:  3.10.110.10
Gene Ontology:  GO:0061657|GO:0071568|GO:1990592
PubMed:  19851334|36645006|32326224|19940261|26463729
SCOP:  4001046

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBCc_UFC1 cd11686
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold ...
 7-157 6.02e-123

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins; UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1.


:

Pssm-ID: 467409  Cd Length: 151  Bit Score: 341.89  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655845775   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDI 86
Cdd:cd11686    1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655845775  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKG 157
Cdd:cd11686   81 PVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
 
Name Accession Description Interval E-value
UBCc_UFC1 cd11686
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold ...
 7-157 6.02e-123

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins; UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1.


Pssm-ID: 467409  Cd Length: 151  Bit Score: 341.89  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655845775   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDI 86
Cdd:cd11686    1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655845775  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKG 157
Cdd:cd11686   81 PVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 6-160 5.21e-119

Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.


Pssm-ID: 400850  Cd Length: 155  Bit Score: 332.33  E-value: 5.21e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655845775    6 TRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFD 85
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIESNKEGTRWFGKCWYVHNLLKYEFDLEFD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655845775   86 IPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQ 160
Cdd:pfam08694  81 IPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
 
Name Accession Description Interval E-value
UBCc_UFC1 cd11686
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold ...
 7-157 6.02e-123

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins; UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1.


Pssm-ID: 467409  Cd Length: 151  Bit Score: 341.89  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655845775   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFDI 86
Cdd:cd11686    1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655845775  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKG 157
Cdd:cd11686   81 PVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 6-160 5.21e-119

Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.


Pssm-ID: 400850  Cd Length: 155  Bit Score: 332.33  E-value: 5.21e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655845775    6 TRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNADNDWFRLESNKEGTRWFGKCWYIHDLLKYEFDIEFD 85
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIESNKEGTRWFGKCWYVHNLLKYEFDLEFD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655845775   86 IPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEIPDLIQKGVIQ 160
Cdd:pfam08694  81 IPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
 
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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