URG1_SCHPO
ID URG1_SCHPO Reviewed; 439 AA.
AC Q9US41;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Uracil-regulated protein 1;
DE EC=3.5.4.-;
GN Name=urg1; ORFNames=SPAC1002.19;
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP INDUCTION.
RX PubMed=18197241; DOI=10.1371/journal.pone.0001428;
RA Watt S., Mata J., Lopez-Maury L., Marguerat S., Burns G., Baehler J.;
RT "urg1: a uracil-regulatable promoter system for fission yeast with short
RT induction and repression times.";
RL PLoS ONE 3:E1428-E1428(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Strongly increased in response to uracil.
CC {ECO:0000269|PubMed:18197241}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. {ECO:0000305}.
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DR EMBL; CU329670; CAB65619.1; -; Genomic_DNA.
DR RefSeq; NP_593508.1; NM_001018942.2.
DR AlphaFoldDB; Q9US41; -.
DR SMR; Q9US41; -.
DR STRING; 4896.SPAC1002.19.1; -.
DR iPTMnet; Q9US41; -.
DR MaxQB; Q9US41; -.
DR PaxDb; Q9US41; -.
DR EnsemblFungi; SPAC1002.19.1; SPAC1002.19.1:pep; SPAC1002.19.
DR GeneID; 2543259; -.
DR KEGG; spo:SPAC1002.19; -.
DR PomBase; SPAC1002.19; urg1.
DR VEuPathDB; FungiDB:SPAC1002.19; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_029639_1_0_1; -.
DR InParanoid; Q9US41; -.
DR OMA; TAYIFGP; -.
DR PhylomeDB; Q9US41; -.
DR PRO; PR:Q9US41; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; -; 1.
DR InterPro; IPR022163; GTP_CH_N.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR Pfam; PF12471; GTP_CH_N; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1..439
FT /note="Uracil-regulated protein 1"
FT /id="PRO_0000353828"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 268..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 315..317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 439 AA; 49035 MW; B2CAF5CD71BF0430 CRC64;
MLATEQSRPA ECNGAHAHEK TEEVKKPLYS RPVVLTTYPS QSRIDPFPMN WGAATAEERG
PITVARSIET LPHRNAVGAH GGSYSVYNAL AVAGGFLPPD HRPNFELTEP TFDFPELDSW
HDPKKIVAMD PYGHLTPSVF KKYLDEGYDV RPTIAITRAH LQVTEIQRSV ENGSLPIDGK
IVLNEKGDIA VTKVAVEPVW YLPGVAERFG VDEVTLRRAL FEQMGGAYPE LITRPDIKVF
LPPIGGLTAY IFGPPEYLSD TSKSLAVRVH DECNGSDVFQ SDICTCRPYL TFGIEEAAKE
AQNGGAGLVV YFRKEGRALG EVVKYLVYNK RKRTGDSAEN YFKRTEELAG VRDMRFQALM
PDILHWFGIK KIDRMLSMSN MKHDAIVGQG IKILNRITIP DDLIPEDSQV EIDAKIQSGY
FSEKKVTEDD LSCVHGRHW
