UBA4_SCHPO
ID UBA4_SCHPO Reviewed; 401 AA.
AC Q09810;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Adenylyltransferase and sulfurtransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Adenylyltransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Sulfurtransferase uba4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_03049};
GN Name=uba4 {ECO:0000255|HAMAP-Rule:MF_03049}; ORFNames=SPAC2G11.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts
CC by mediating the C-terminal thiocarboxylation of sulfur carrier URM1.
CC Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then
CC the persulfide sulfur on the catalytic cysteine is transferred to URM1
CC to form thiocarboxylation (-COSH) of its C-terminus. The reaction
CC probably involves hydrogen sulfide that is generated from the
CC persulfide intermediate and that acts as nucleophile towards URM1.
CC Subsequently, a transient disulfide bond is formed. Does not use
CC thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for
CC thiocarboxylation reactions. Prior mcm(5) tRNA modification by the
CC elongator complex is required for 2-thiolation. May also be involved in
CC protein urmylation. {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC family. UBA4 subfamily. {ECO:0000255|HAMAP-Rule:MF_03049}.
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DR EMBL; CU329670; CAA91175.1; -; Genomic_DNA.
DR PIR; S62465; S62465.
DR RefSeq; NP_593090.1; NM_001018488.2.
DR AlphaFoldDB; Q09810; -.
DR SMR; Q09810; -.
DR BioGRID; 278233; 21.
DR STRING; 4896.SPAC2G11.10c.1; -.
DR MaxQB; Q09810; -.
DR PaxDb; Q09810; -.
DR EnsemblFungi; SPAC2G11.10c.1; SPAC2G11.10c.1:pep; SPAC2G11.10c.
DR GeneID; 2541739; -.
DR KEGG; spo:SPAC2G11.10c; -.
DR PomBase; SPAC2G11.10c; -.
DR VEuPathDB; FungiDB:SPAC2G11.10c; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR InParanoid; Q09810; -.
DR OMA; PEWPIRC; -.
DR PhylomeDB; Q09810; -.
DR Reactome; R-SPO-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q09810; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0070733; F:protein adenylyltransferase activity; ISO:PomBase.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; ISO:PomBase.
DR GO; GO:0042292; F:URM1 activating enzyme activity; ISO:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:PomBase.
DR GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; ISO:PomBase.
DR Gene3D; 3.40.250.10; -; 1.
DR HAMAP; MF_03049; MOCS3_Uba4; 1.
DR InterPro; IPR028885; MOCS3/Uba4.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase; tRNA processing;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..401
FT /note="Adenylyltransferase and sulfurtransferase uba4"
FT /id="PRO_0000120581"
FT DOMAIN 313..399
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 198
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 358
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 81..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 142..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
SQ SEQUENCE 401 AA; 44416 MW; 31AE51EECC0B2EA3 CRC64;
MNPQEKIICS SNGLELSLDE YSRYGRQMLL SEIGLPGQLS LKRSSVLVIG AGGLGCPAMQ
YLVAAGIGTL GIMDGDVVDK SNLHRQIIHS TSKQGMHKAI SAKQFLEDLN PNVIINTYLE
FASASNLFSI IEQYDVVLDC TDNQYTRYLI SDTCVLLGRP LVSASALKLE GQLCIYNYCN
GPCYRCMFPN PTPVVASCAK SGILGPVVGT MGTMQALETV KLILHINGIK KDQFDPYMLL
FHAFKVPQWK HIRIRPRQQS CKACGPNKML SREFMESSPK EYTTICDYVP TLSKQLAPIR
RISALDLKNL IETSPHITFL DVREPVQFGI CRLPLFKNIP LSEVDSLQNL SGKVCVICRS
GNTSQTAVRK LQELNPQADI FDVVAGLKGW STEVDPNFPL Y
