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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//