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Database: UniProt
Entry: Q5JZT9_MEDTR
LinkDB: Q5JZT9_MEDTR
Original site: Q5JZT9_MEDTR 
ID   Q5JZT9_MEDTR            Unreviewed;       418 AA.
AC   Q5JZT9; A0A0C3XUD6; G7K4A9;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Cell division FtsZ-like protein {ECO:0000313|EMBL:AET00625.2};
DE   SubName: Full=Plastid division protein {ECO:0000313|EMBL:CAI44667.1};
GN   Name=ftsz1 {ECO:0000313|EMBL:CAI44667.1};
GN   Synonyms=11433055 {ECO:0000313|EnsemblPlants:AET00625};
GN   OrderedLocusNames=MTR_5g094120 {ECO:0000313|EMBL:AET00625.2};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:CAI44667.1};
RN   [1] {ECO:0000313|EMBL:CAI44667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A17 {ECO:0000313|EMBL:CAI44667.1};
RX   PubMed=16854943; DOI=10.1093/pcp/pcj083;
RA   Lohse S., Hause B., Hause G., Fester T.;
RT   "FtsZ characterization and immunolocalization in the two phases of plastid
RT   reorganization in arbuscular mycorrhizal roots of Medicago truncatula.";
RL   Plant Cell Physiol. 47:1124-1134(2006).
RN   [2] {ECO:0000313|EMBL:AET00625.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AET00625.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AET00625,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [3] {ECO:0000313|EMBL:AET00625.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET00625,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [4] {ECO:0000313|EnsemblPlants:AET00625}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET00625};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the FtsZ family.
CC       {ECO:0000256|ARBA:ARBA00009690}.
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DR   EMBL; CM001221; AET00625.2; -; Genomic_DNA.
DR   EMBL; AJ875090; CAI44667.1; -; mRNA.
DR   RefSeq; XP_003617666.2; XM_003617618.2.
DR   AlphaFoldDB; Q5JZT9; -.
DR   STRING; 3880.Q5JZT9; -.
DR   PaxDb; 3880-AET00625; -.
DR   EnsemblPlants; AET00625; AET00625; MTR_5g094120.
DR   GeneID; 11433055; -.
DR   Gramene; AET00625; AET00625; MTR_5g094120.
DR   KEGG; mtr:11433055; -.
DR   eggNOG; ENOG502QRFN; Eukaryota.
DR   HOGENOM; CLU_024865_0_0_1; -.
DR   OrthoDB; 10064at2759; -.
DR   Proteomes; UP000002051; Chromosome 5.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0010020; P:chloroplast fission; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02201; FtsZ_type1; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   HAMAP; MF_00909; FtsZ; 1.
DR   InterPro; IPR000158; Cell_div_FtsZ.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR045061; FtsZ/CetZ.
DR   InterPro; IPR024757; FtsZ_C.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   NCBIfam; TIGR00065; ftsZ; 1.
DR   PANTHER; PTHR30314:SF12; CELL DIVISION PROTEIN FTSZ HOMOLOG 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR   Pfam; PF12327; FtsZ_C; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle {ECO:0000313|EMBL:AET00625.2};
KW   Cell division {ECO:0000313|EMBL:AET00625.2};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          61..253
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          255..372
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          387..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  43978 MW;  21FB699B152A8927 CRC64;
     MVTTLLPSSL TNPNKLLSHS SLFHNSSLST SHSVSLYPKT QRFTRRFGSV KCSLAYVDNA
     KIKVVGIGGG GNNAVNRMIG SGLQGVDFYA INTDAQALLH SAAENPIKIG ELLTRGLGTG
     GNPLLGEQAA EESKEAIADA LKGSDLVFIT AGMGGGTGSG AAPVVAQISK EAGYLTVGVV
     TYPFSFEGRK RSLQALEAIE KLQRNVDTLI VIPNDRLLDI ADEQMPLQDA FRLADDVLRQ
     GVQGISDIIT IPGLVNVDFA DVKAVMKDSG TAMLGVGVSS GKNRAEEAAE QATLAPLIGS
     SIQSATGVVY NITGGKDITL QEVNRVSQVV TSLADPSANI IFGAVVDDRY TGEIHVTIIA
     TGFSQSFQKK LLTDPRAAKL LDKVAEGKES KTVPAPLKSS NLSSKVESRA PPPRKLFF
//
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