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Database: UniProt
Entry: K3XV53_SETIT
LinkDB: K3XV53_SETIT
Original site: K3XV53_SETIT 
ID   K3XV53_SETIT            Unreviewed;       913 AA.
AC   K3XV53;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=101764728 {ECO:0000313|EnsemblPlants:KQL10137};
GN   ORFNames=SETIT_4G108600v2 {ECO:0000313|EMBL:RCV21075.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL10137, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EMBL:RCV21075.1, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL10137,
RC   ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC   {ECO:0000313|EMBL:RCV21075.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV21075.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV21075.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQL10137}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL10137};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001837};
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR   EMBL; AGNK02002327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM003531; RCV21075.1; -; Genomic_DNA.
DR   RefSeq; XP_004965129.1; XM_004965072.1.
DR   AlphaFoldDB; K3XV53; -.
DR   STRING; 4555.K3XV53; -.
DR   EnsemblPlants; KQL10137; KQL10137; SETIT_005810mg.
DR   GeneID; 101764728; -.
DR   Gramene; KQL10137; KQL10137; SETIT_005810mg.
DR   KEGG; sita:101764728; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_016157_1_0_1; -.
DR   InParanoid; K3XV53; -.
DR   OMA; KMVRKPI; -.
DR   OrthoDB; 1209347at2759; -.
DR   Proteomes; UP000004995; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   CDD; cd08771; DLP_1; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF147; DYNAMIN GTPASE; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004995}.
FT   DOMAIN          35..307
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          576..698
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          737..830
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          511..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  99677 MW;  AC3A025DE2EEE264 CRC64;
     MEAIEELSEL SESMRQAASL LADDDPSDEA APRRPTTFLN AVALGNVGAG KSAVLNSLIG
     HPVLPTGENG ATRAPIVVDL QREPGLSSKS IVLQIDSKSQ QVTASALRHS LQDRLSKGAS
     GGSGRGRGDE IYLKLRTSTA PPLKLIDLPG IDQRAVDDSV INEYAGHNDA ILLVVIPAMQ
     AADVASSRAL RLAKDIDSDG TRTVGVISKV DQANGDAKTI ACVQALLSNK GPKNLPDIEW
     VALIGQSVAI ASAQSVGSEN SLETAWRAEA ETLKSILTGA PQNKLGRLAL VDTIAKQIRK
     RMKVRLPNLL SGLQGKSQMV QDELARLGES MVQSPEGTRA VALELCREFE DKFLAHITSG
     EGSGWKIVAS FEGKFPDRIK QLPLDRHFDL NNVKRIVLEA DGYQPYLISP EKGLRSLIKI
     VLEMAKEPSR LCVEEVHRVL LDIINASANA TPGLGRYPPF KREVVAIASN ALESFKNDAK
     KMVVALVDME RAFVPPQHFI RLVQRRMERQ RREDELKNRS SKKTQEAEQS MSKRASSPQT
     DSEQGGGSLK SMKDKSGQQD KDTKEGSNLQ VAGPAGEITA GYLLKKSAKT NGWSKRWFVL
     NEKSGKLGYT KKQEERHFRG VITLEECNLE EVEEEEPSKS SKDSKKANGP EKTPSLVFKI
     TNRVAYKTVL KAHSAVVLKA ESMSDKVEWV NKIKAVIQSK GGSFKGPNTE GGSMRQSHSD
     GSLDTMARRP ADPEEELRWM SQEVRGYVEA VLNSLAANVP KAIVLCQVEK AKEDMLNQLY
     SSISGQSNAK IEELLQEDHN AKRRREKYQK QSSLLSKLTR QLSIHDNRAS VSSYSNDTSE
     AESPRTPSRS GEDWRSAFDS ASNGPPAASS NSESRSRSAD GRSRRYENGD VSAGANSGSR
     RTPNRLPPAP PRY
//
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