DPH6_SCHPO
ID DPH6_SCHPO Reviewed; 606 AA.
AC Q9USQ7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Diphthine--ammonia ligase;
DE EC=6.3.1.14;
DE AltName: Full=Diphthamide synthase;
DE AltName: Full=Diphthamide synthetase;
GN Name=mug71; ORFNames=SPBC577.12;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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).
CC -!- FUNCTION: Amidase that catalyzes the last step of diphthamide
CC biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists
CC in the conversion of an L-histidine residue in the translation
CC elongation factor eEF-2 (eft201 or eft202) to diphthamide (By
CC similarity). Has a role in meiosis. {ECO:0000250,
CC ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC ChEBI:CHEBI:456215; EC=6.3.1.14;
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the Diphthine--
CC ammonia ligase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RutC family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB54820.1; -; Genomic_DNA.
DR PIR; T40556; T40556.
DR RefSeq; NP_595310.1; NM_001021217.2.
DR AlphaFoldDB; Q9USQ7; -.
DR SMR; Q9USQ7; -.
DR BioGRID; 277240; 14.
DR STRING; 4896.SPBC577.12.1; -.
DR MaxQB; Q9USQ7; -.
DR PaxDb; Q9USQ7; -.
DR PRIDE; Q9USQ7; -.
DR EnsemblFungi; SPBC577.12.1; SPBC577.12.1:pep; SPBC577.12.
DR GeneID; 2540717; -.
DR KEGG; spo:SPBC577.12; -.
DR PomBase; SPBC577.12; -.
DR VEuPathDB; FungiDB:SPBC577.12; -.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_010289_2_1_1; -.
DR InParanoid; Q9USQ7; -.
DR OMA; RNTMHVQ; -.
DR PhylomeDB; Q9USQ7; -.
DR Reactome; R-SPO-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:Q9USQ7; -.
DR Proteomes; UP000002485; Chromosome II.
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:0017178; F:diphthine-ammonia ligase activity; ISO:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISO:PomBase.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IC:PomBase.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR Gene3D; 3.30.1330.40; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR12196; PTHR12196; 1.
DR Pfam; PF01902; Diphthami_syn_2; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 2.
DR SUPFAM; SSF55298; SSF55298; 2.
DR TIGRFAMs; TIGR00290; MJ0570_dom; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..606
FT /note="Diphthine--ammonia ligase"
FT /id="PRO_0000278564"
SQ SEQUENCE 606 AA; 67624 MW; 059CE8F3A651F599 CRC64;
MKVLGLISGG KDSCFNLMHC VSLGHEVVAL ANLHPEDGKD EIDSFMYQSV GHDVIPLYAE
CFDLPLYREK IGGQSINQNL DYQFTEKDET EDLYRLIKRV LTNHPDLEAV STGAILSTYQ
RTRVENVCKR LGLKSLSFLW QKDQEKLLND MVVSGLNAIL IKVAAIGLTR KDLGKSLAEM
QDKLLTLNKK FELHPCGEGG EYETLVLDCP LFKKRIVLTD KEVVEHSSGE VCYLKVKACV
KDKPEWQPIS LKSELVPNEE LLGEEYSHIY HTISKKYELI DDQEETPTSL IPIPLRESAF
QQKKGSFLVL GNVVATKGSY NTFQGEAESA INNLNELLGT YGYSNKNVYF VTVILSSMSK
FAEFNSVYNK YFDFTNPPSR SCVAAPLASE YRIVMSCIVG DVTEKRALHV QGQSYWAPAN
IGPYSQSICA NGVVFISGQI GLIPSVMELK LHDKIFEMVL ALQHANRVAK AMRVGSLIAC
LAYVCDSRDA DCVVKIWSEY TKNTGESSPV LVALVDALPR NASVEWQLLY NDSSCDVPLL
SSLVTNQTLF GSDTAWDVAL LNQNGLRMES SFIHHEHPSA YAIVLNNAFP NSQLLHVRYT
ARDQNV
