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Database: UniProt
Entry: F4JHA4_ARATH
LinkDB: F4JHA4_ARATH
Original site: F4JHA4_ARATH 
ID   F4JHA4_ARATH            Unreviewed;       816 AA.
AC   F4JHA4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN   Name=RSH1 {ECO:0000313|EMBL:AEE82146.1, ECO:0000313|TAIR:AT4G02260};
GN   Synonyms=AT-RSH1 {ECO:0000313|EMBL:AEE82146.1}, ATRSH1
GN   {ECO:0000313|EMBL:AEE82146.1}, RELA-SPOT HOMOLOG 1
GN   {ECO:0000313|EMBL:AEE82146.1}, RELA/SPOT HOMOLOG 1
GN   {ECO:0000313|EMBL:AEE82146.1}, RELA/SPOT homolog 1
GN   {ECO:0000313|EMBL:AEE82146.1};
GN   OrderedLocusNames=At4g02260 {ECO:0000313|Araport:AT4G02260,
GN   ECO:0000313|EMBL:AEE82146.1};
GN   ORFNames=T2H3.10 {ECO:0000313|EMBL:AEE82146.1}, T2H3_10
GN   {ECO:0000313|EMBL:AEE82146.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE82146.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE82146.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA   Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA   Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA   Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA   Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA   Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA   Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA   Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA   Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA   Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA   Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA   Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC       {ECO:0000256|ARBA:ARBA00007476}.
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DR   EMBL; CP002687; AEE82146.1; -; Genomic_DNA.
DR   RefSeq; NP_974501.1; NM_202772.2.
DR   AlphaFoldDB; F4JHA4; -.
DR   SMR; F4JHA4; -.
DR   ProteomicsDB; 197653; -.
DR   EnsemblPlants; AT4G02260.3; AT4G02260.3; AT4G02260.
DR   GeneID; 828096; -.
DR   Gramene; AT4G02260.3; AT4G02260.3; AT4G02260.
DR   Araport; AT4G02260; -.
DR   TAIR; AT4G02260; RSH1.
DR   HOGENOM; CLU_012300_5_0_1; -.
DR   OMA; HSIQWFC; -.
DR   PhylomeDB; F4JHA4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JHA4; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   PANTHER; PTHR43061; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43061:SF1; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   1: Evidence at protein level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F4JHA4,
KW   ECO:0007829|ProteomicsDB:F4JHA4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          172..279
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          562..625
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   REGION          710..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  91647 MW;  FA75F6CA92B054F8 CRC64;
     MTSASSMSVS VECVNICNLT KGDGNARSDC SALSCAWKAP RALTGFLAST AHPPVCSVYS
     CGRNGRKSRM KACAWQRYEY EVGFSEAPYF VNVRNILKSR LSCGGHKRWE LYCVSAESSS
     GASSDVTVET LWEDLFPSIS YLPRKELEFV QKGLKLAFEA HHGQKRRSGE PFIIHPVAVA
     RILGELELDW ESIVAGLLHD TVEDTNFITF EKIEEEFGAT VRHIVEGETK VSKLGKLKCK
     TESETIQDVK ADDLRQMFLA MTDEVRVIIV KLADRLHNMR TLCHMPPHKQ SSIAGETLQV
     FAPLAKLLGM YSIKSELENL SFMYVSAEDY DRVTSRIANL YKEHEKELTE ANRILVKKIE
     DDQFLDLVTV NTDVRSVCKE TYSIYKAALK SKGSINDYNQ IAQLRIVVKP KPSVGVGPLC
     SPQQICYHVL GLVHEIWKPI PRTVKDYIAT PKPNGYQSLH TTVIPFLYES MFRLEVQIRT
     EEMDLIAERG IAVYYNGKSL STGLVGNAVP LGRNSRGKTG CLNNADFALR VGWLNAIREW
     QEEFVGNMSS REFVDTITRD LLGSRVFVFT PKGEIKNLPK GATVVDYAYL IHTEIGNKMV
     AAKVNGNLVS PTHVLENAEV VEIVTYNALS SKSAFQRHKQ WLQHAKTRSA RHKIMRFLRE
     QAAQCAAEIT QDQVNDFVAD SDSDVEDLTE DSRKSLQWWE KILVNVKQFQ SQDKSRDTTP
     APQNGSVWAP KVNGKHNKAI KNSSSDEPEF LLPGDGIARI LPANIPAYKE VLPGLDSWRD
     SKIATWHHLE GQSIEWLCVV SMDRKGMGIF VLFSHD
//
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