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Conserved domains on  [gi|1344537312|ref|NP_001347860|]
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ubiquitin-fold modifier-conjugating enzyme 1 isoform a [Mus musculus]

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 3.46e-122

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: 340.35  E-value: 3.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFEI 86
Cdd:cd11686     1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1344537312  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKG 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 3.46e-122

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: 340.35  E-value: 3.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFEI 86
Cdd:cd11686     1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1344537312  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKG 157
Cdd:cd11686    81 PVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 6-160 4.01e-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: 332.72  E-value: 4.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312   6 TRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFE 85
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIESNKEGTRWFGKCWYVHNLLKYEFDLEFD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344537312  86 IPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKGVIQ 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 3.46e-122

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: 340.35  E-value: 3.46e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312   7 RRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFEI 86
Cdd:cd11686     1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIESNKEGTRWFGKCWYIHNLLKYEFDLEFDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1344537312  87 PITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKG 157
Cdd:cd11686    81 PVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 6-160 4.01e-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: 332.72  E-value: 4.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312   6 TRRVVSEIPVLKTNAGPRDRELWVQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEGTRWFGKCWYIHDFLKYEFDIEFE 85
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIESNKEGTRWFGKCWYVHNLLKYEFDLEFD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344537312  86 IPITYPTTAPEIAVPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGLAHLMALGLGPWLAVEVPDLIQKGVIQ 160
Cdd:pfam08694  81 IPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 30-125 3.19e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


Pssm-ID: 467407 [Multi-domain]  Cd Length: 112  Bit Score: 35.73  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344537312  30 QRLKEEYQSLiryvennKNSDNDWFRLESNKEG-TRWFGKCWYIHD--FLKYEFDIEFEIPITYPTTAPEIAVpeldgKT 106
Cdd:cd00195     1 KRLQKELKEL-------QKNPPPGISVEPVDDDlFHWKATIKGPEGtpYEGGVFKLDIEFPDDYPFKPPKVRF-----LT 68

                          90       100
                  ....*....|....*....|....
gi 1344537312 107 aKMY-----RGGKICLTDHFKPLW 125
Cdd:cd00195    69 -PIYhpnvdPDGEICLDILKSEGW 91
SLATT_5 pfam18160
SMODS and SLOG-associating 2TM effector domain family 5; The SLATT domain contains two ...
 7-80 6.32e-03

SMODS and SLOG-associating 2TM effector domain family 5; The SLATT domain contains two transmembrane helices. SLATT domains are generally predicted to function as pore-forming effectors in a class of conflict systems which are reliant on the production of second messenger nucleotide or nucleotide derivatives. SLATT domains are predicted to initiate cell suicide responses upon their activation. This SLATT family contains an additional C-terminal alpha-helix, and strictly associates with a reverse transcriptase domain, part of a predicted retroelement with diversity-generating potential.


Pssm-ID: 436319  Cd Length: 191  Bit Score: 35.76  E-value: 6.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1344537312   7 RRVVSEIPVLKTNAGPRDRELwvQRLKEEYQSLIRYVENNKNSDNDWFRLESNKEgtRWFGKCWYIHDFLKYEF 80
Cdd:pfam18160 102 SRLYNELQLLLISEDDLKEKY--KDISKEYEEILDKYENHSPIDYKLFRSESLKS--EPLGKWRKIRWFLLRYI 171
 
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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