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Information on EC 2.7.7.100 - SAMP-activating enzyme
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2.7.7.100 SAMP-activating enzymeIUBMB Comments
Contains Zn2+. The enzyme catalyses the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea, by catalysing the ATP-dependent formation of a SAMP adenylate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage. The product of this activity can accept a sulfur atom to form a thiocarboxylate moiety that acts as a sulfur carrier involved in thiolation of tRNA and other metabolites such as molybdopterin. Alternatively, the enzyme can also catalyse the transfer of SAMP from its activated form to an internal cysteine residue, leading to a process termed SAMPylation (see EC 6.2.1.55, E1 SAMP-activating enzyme).
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The expected taxonomic range for this enzyme is: Halobacteria
Reaction Schemes
+
[SAMP]-Gly-Gly
=
+
[SAMP]-Gly-Gly-AMP
Synonyms
ubiquitin-activating e1 enzyme homolog, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E1-like enzyme
E1-like UbaA
E1-like ubiquitin-activating homolog
SAMP-activating E1 enzyme
SAMP-activating enzyme E1
-
-
ambiguous
-
UbaA
ubiquitin-activating E1 enzyme homolog
SAMP-activating E1 enzyme
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
UbaA
-
-
ambiguous
-
UbaA
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [SAMP]-Gly-Gly = diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[SAMP]-Gly-Gly adenylyltransferase
Contains Zn2+. The enzyme catalyses the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea, by catalysing the ATP-dependent formation of a SAMP adenylate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage. The product of this activity can accept a sulfur atom to form a thiocarboxylate moiety that acts as a sulfur carrier involved in thiolation of tRNA and other metabolites such as molybdopterin. Alternatively, the enzyme can also catalyse the transfer of SAMP from its activated form to an internal cysteine residue, leading to a process termed SAMPylation (see EC 6.2.1.55, E1 SAMP-activating enzyme).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [SAMP1]-Gly-Gly
diphosphate + [SAMP1]-Gly-Gly-AMP
-
-
-
?
ADP + [SAMP]-Gly-Gly
phosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP2]-Gly-Gly
diphosphate + [SAMP2]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP2]-Gly-Gly
diphosphate + [SAMP2]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
additional information
?
-
no activity with AMP, CTP, GTP, UTP, and TTP
-
-
?
additional information
?
-
no activity with AMP, CTP, GTP, UTP, and TTP
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [SAMP1]-Gly-Gly
diphosphate + [SAMP1]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP2]-Gly-Gly
diphosphate + [SAMP2]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP2]-Gly-Gly
diphosphate + [SAMP2]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
ATP + [SAMP]-Gly-Gly
diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme is required for SAMPylation and molybdenum cofactor biosynthesis
metabolism
UbaA mediates covalent and non-covalent associations of NcsA with SAMP2
metabolism
-
UbaA mediates covalent and non-covalent associations of NcsA with SAMP2
-
physiological function
the enzyme is crucial for optimal growth at high temperature
physiological function
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
physiological function
-
in archaea, E1-like enzymes, such as Haloferax volcanii UbaA, are central hubs that activate the Ubls for ligation to protein targets and for sulfur mobilization. UbaA is required for the Ubl small archaeal modifier proteins (SAMPs) to serve as protein modifiers and to carry sulfur to biomolecules. SAMP1 carries sulfur to form Moco, based on its binding to MoaE (the large subunit of molybdopterin [MPT] synthase) and its requirement for Moco-dependent dimethyl sulfoxide (DMSO) reductase activity. Haloferax volcanii UbaA is not fused to an RHD. The stand-alone rhodanese-like domain (RHD) protein UbaC (UniProt ID D4GTH6) plays a role in ubiquitin-like protein modification and sulfur mobilization in Archaea. UbaC of Haloferax volcanii binds the E1 UbaA and is required for Ubl modification and for functions associated with Ubl sulfur relay. UbaC and its conserved active-site cysteine(C64) are (i) required for DMSO respiration/reductase activity correlated with Moco biosynthesis, (ii) important for survival at elevated temperature, which is indicative of a functional wobble uridine tRNA thiolation pathway, and (iii) critical for the formation of Ubl ligation products, with marked exception of the SAMP1 conjugates induced by oxidative stress. E1-RHD relationship, detailed overview
-
additional information
UbaA-UbaC interaction analysis by pulldown assay
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
additional information
-
UbaA-UbaC interaction analysis by pulldown assay
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UBAA_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
270
0
28704
Swiss-Prot
other Location (Reliability: 3)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
additional information
-
generation of DELTAubaC, DELTAsamp1, and DELTAubaA mutants that are unable to grow on DMSO. When ubaC is expressed in trans, the DELTAubaC mutant is restored for anaerobic respiration on DMSO, revealing that the effect is specific to ubaC, the UbaC C64S variant does not complement the DELTAubaC mutation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of UbaA, co-purification with StrepII-tagged rhodanese-like domain protein UbaC
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miranda, H.; Antelmann, H.; Hepowit, N.; Chavarria, N.; Krause, D.; Pritz, J.; Bäsell, K.; Becher, D.; Humbard, M.; Brocchieri, L.; Maupin-Furlow, J.
Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism
Mol. Cell. Proteomics
13
220-239
2014
Haloferax volcanii
brenda
Dantuluri, S.; Wu, Y.; Hepowit, N.L.; Chen, H.; Chen, S.; Maupin-Furlow, J.A.
Proteome targets of ubiquitin-like samp1ylation are associated with sulfur metabolism and oxidative stress in Haloferax volcanii
Proteomics
16
1100-1110
2016
Haloferax volcanii (D4GSF3), Haloferax volcanii YW1001 (D4GSF3)
brenda
Bochtler, M.; Piasecka, A.
Haloferax volcanii UbaA, catalytic engine for sampylation and sulfur transfer
FEBS J.
283
3563-3566
2016
Haloferax volcanii
brenda
Hepowit, N.; de Vera, I.; Cao, S.; Fu, X.; Wu, Y.; Uthandi, S.; Chavarria, N.; Englert, M.; Su, D.; Soell, D.; Kojetin, D.; Maupin-Furlow, J.
Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of Archaea
FEBS J.
283
3567-3586
2016
Haloferax volcanii (D4GSF3), Haloferax volcanii ATCC 29605 (D4GSF3)
brenda
Chavarria, N.; Hwang, S.; Cao, S.; Fu, X.; Holman, M.; Elbanna, D.; Rodriguez, S.; Arrington, D.; Englert, M.; Uthandi, S.; Soell, D.; Maupin-Furlow, J.
Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is associated with ubiquitin-proteasome, translation, and RNA processing system homologs
PLoS ONE
9
e99104
2014
Haloferax volcanii (D4GSF3), Haloferax volcanii ATCC 29605 (D4GSF3)
brenda
Miranda, H.; Nembhard, N.; Su, D.; Hepowit, N.; Krause, D.; Pritz, J.; Phillips, C.; Sll, D.; Maupin-Furlow, J.
E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea
Proc. Natl. Acad. Sci. USA
108
4417-4422
2011
Haloferax volcanii (D4GSF3)
brenda
Maupin-Furlow, J.
Archaeal proteasomes and sampylation
Subcell. Biochem.
66
297-327
2013
Haloferax volcanii (D4GSF3)
brenda
Maupin-Furlow, J.
Ubiquitin-like proteins and their roles in archaea
Trends Microbiol.
21
31-38
2013
Haloferax volcanii (D4GSF3)
brenda
Hepowit, N.; Maupin-Furlow, J.
Rhodanese-like domain protein UbaC and its role in ubiquitin-Like protein modification and sulfur mobilization in Archaea
J. Bacteriol.
201
e00254-19
2019
Haloferax volcanii (D4GSF3), Haloferax volcanii NCIMB 2012 (D4GSF3), Haloferax volcanii JCM 8879 (D4GSF3), Haloferax volcanii DS2 (D4GSF3), Haloferax volcanii DSM 3757 (D4GSF3), Haloferax volcanii ATCC 29605 (D4GSF3), Haloferax volcanii NBRC 14742 (D4GSF3), Haloferax volcanii VKM B-1768 (D4GSF3)
brenda
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