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Adenylyltransferase and sulfurtransferase UBA4 (Ubiquitin-like protein activator 4) [Includes: Adenylyltransferase UBA4 (EC 2.7.7.-); Sulfurtransferase UBA4 (EC 2.8.1.-)]

 A0A1V1T0S6_9FUNG        Unreviewed;       486 AA.
A0A1V1T0S6;
07-JUN-2017, integrated into UniProtKB/TrEMBL.
07-JUN-2017, sequence version 1.
28-MAR-2018, entry version 9.
RecName: Full=Adenylyltransferase and sulfurtransferase UBA4 {ECO:0000256|HAMAP-Rule:MF_03049};
AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000256|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Sulfurtransferase UBA4 {ECO:0000256|HAMAP-Rule:MF_03049};
EC=2.8.1.- {ECO:0000256|HAMAP-Rule:MF_03049};
Includes:
RecName: Full=Adenylyltransferase UBA4 {ECO:0000256|HAMAP-Rule:MF_03049};
EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_03049};
Name=UBA4 {ECO:0000256|HAMAP-Rule:MF_03049};
ORFNames=ANO14919_038490 {ECO:0000313|EMBL:GAW14446.1};
fungal sp. No.14919.
Eukaryota; Fungi.
NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW14446.1, ECO:0000313|Proteomes:UP000189293};
[1] {ECO:0000313|EMBL:GAW14446.1, ECO:0000313|Proteomes:UP000189293}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=No.14919 {ECO:0000313|EMBL:GAW14446.1,
ECO:0000313|Proteomes:UP000189293};
Technology Reseach Association of Highly Efficient Gene Design;
Itoh H., Matsui M., Shibata T.;
Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:GAW14446.1, ECO:0000313|Proteomes:UP000189293}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=No.14919 {ECO:0000313|EMBL:GAW14446.1,
ECO:0000313|Proteomes:UP000189293};
Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
"Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
Inhibitor FR901512.";
Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at
tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and
tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of
sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-
adenylate (-COAMP), then the persulfide sulfur on the catalytic
cysteine is transferred to URM1 to form thiocarboxylation (-COSH)
of its C-terminus. The reaction probably involves hydrogen sulfide
that is generated from the persulfide intermediate and that acts
as nucleophile towards URM1. Subsequently, a transient disulfide
bond is formed. Does not use thiosulfate as sulfur donor; NFS1
probably acting as a sulfur donor for thiocarboxylation reactions.
Prior mcm(5) tRNA modification by the elongator complex is
required for 2-thiolation. May also be involved in protein
urmylation. {ECO:0000256|HAMAP-Rule:MF_03049}.
-!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
tRNA biosynthesis. {ECO:0000256|SAAS:SAAS00337567}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00135658}.
-!- SIMILARITY: In the N-terminal section; belongs to the
HesA/MoeB/ThiF family. UBA4 subfamily.
{ECO:0000256|SAAS:SAAS00535337}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:GAW14446.1}.
-----------------------------------------------------------------------
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EMBL; BDMC01000009; GAW14446.1; -; Genomic_DNA.
UniPathway; UPA00988; -.
Proteomes; UP000189293; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
GO; GO:0018192; P:enzyme active site formation via cysteine modification to L-cysteine persulfide; IEA:UniProtKB-UniRule.
GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
Gene3D; 3.40.250.10; -; 1.
HAMAP; MF_03049; MOCS3_Uba4; 1.
InterPro; IPR028885; MOCS3/Uba4.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
InterPro; IPR000594; ThiF_NAD_FAD-bd.
InterPro; IPR035985; Ubiquitin-activating_enz.
Pfam; PF00581; Rhodanese; 1.
Pfam; PF00899; ThiF; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF69572; SSF69572; 1.
PROSITE; PS50206; RHODANESE_3; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885939}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000189293};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416191};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00001785};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416195};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885939};
Reference proteome {ECO:0000313|Proteomes:UP000189293};
Transferase {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00885834};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_03049,
ECO:0000256|SAAS:SAAS00416193};
Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_03049};
Zinc {ECO:0000256|HAMAP-Rule:MF_03049, ECO:0000256|SAAS:SAAS00001782}.
DOMAIN 376 484 Rhodanese. {ECO:0000259|PROSITE:PS50206}.
NP_BIND 128 132 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
NP_BIND 189 190 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
COILED 1 35 {ECO:0000256|SAM:Coils}.
ACT_SITE 255 255 Glycyl thioester intermediate; for
adenylyltransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
ACT_SITE 439 439 Cysteine persulfide intermediate; for
sulfurtransferase activity.
{ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 238 238 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 241 241 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 323 323 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
METAL 326 326 Zinc. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 100 100 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 121 121 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
BINDING 145 145 ATP. {ECO:0000256|HAMAP-Rule:MF_03049}.
SEQUENCE 486 AA; 52112 MW; 35D3EFAB152043FD CRC64;
MDSVTGKVER LKAQISKTEV ELQQLRAQLA ELEGLRPPST PLSPAPQAQD QPTEISQDWK
WPLQEEEYAR YGRQLVLPSV GIRGQLRLKS AAVLVVGAGG LGCPAAAYLA GAGVGTLGVV
DGDTVEVSNL HRQIAHNTAR VGMKKVHSLI QYCQGLNPEV KYIGYDEHLT PQNAEDVVST
YDVVLDCTDH PTSRYLISDI CVLLGKPLVS ASALRTDGQL IVLNNPPAAQ GSADGGPCYR
CVFPKPPPAD SVVSCGEGGI LGPVVGVMGV LQALEAIKLI AAGIGKENGS VSKEPVTPSL
LLFSANSSTP FRSIKMRGRR SNCFACSASS TLTLKELKAG SLDYVQFCGV TQPISILQPD
ERISATYYKS ILASGTEGRS LLLDVREKEH FDVAQIPGAI NIPFSAFQTK SRSTSNGDAP
RLEWLPEDVA SDASIYVVCR VGNDSQLVAK KLKDMGLDRH GERFIGDIKG GMKAWKLEVD
QTMPFT


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