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Database: UniProt
Entry: A0A1S3VHA0_VIGRR
LinkDB: A0A1S3VHA0_VIGRR
Original site: A0A1S3VHA0_VIGRR 
ID   A0A1S3VHA0_VIGRR        Unreviewed;       410 AA.
AC   A0A1S3VHA0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cell division protein FtsZ homolog 1, chloroplastic {ECO:0000313|RefSeq:XP_014517587.1};
GN   Name=LOC106775064 {ECO:0000313|RefSeq:XP_014517587.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014517587.1};
RN   [1] {ECO:0000313|RefSeq:XP_014517587.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014517587.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the FtsZ family.
CC       {ECO:0000256|ARBA:ARBA00009690}.
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DR   RefSeq; XP_014517587.1; XM_014662101.2.
DR   AlphaFoldDB; A0A1S3VHA0; -.
DR   STRING; 3916.A0A1S3VHA0; -.
DR   GeneID; 106775064; -.
DR   KEGG; vra:106775064; -.
DR   OrthoDB; 10064at2759; -.
DR   Proteomes; UP000087766; Chromosome 10.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|RefSeq:XP_014517587.1};
KW   Cell division {ECO:0000313|RefSeq:XP_014517587.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          55..247
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          249..366
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          378..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  43003 MW;  A4F17EDEB0797B24 CRC64;
     MAMLALTNPT SIRHNAFSYS SSSSSFALRT RTCVTARRRF ASVRCCSFST PESAKIKVVG
     VGGGGNNAVN RMIGCGLHGV EFYAINTDAQ ALLHSAAENP IKIGELLTRG LGTGGNPLLG
     EQAAEESKDA IASALQGSDL VFITAGMGGG TGSGAAPVVA RVAKEAGYLT VGVVTYPFSF
     EGRKRSLQAL EAIEKLQKNV DTLIVIPNDR LLDMADEQTP LQDAFRLADD VLRQGVQGIS
     DIITIPGLVN VDFADVKAVM KDSGTAMLGV GVSSSKNRAE EAAEQATLAP LIGSSIQSAT
     GVVYNITGGK DITLQEVNRV SQVVTSLADP SANIIFGAVV DDRYNGEIHV TIIATGFSQS
     FQKTLLTDPR AAKLLDRVPE GQESKAASSS LKSSNYPTLG SRASPRKLFF
//
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