ID D7TGM4_VITVI Unreviewed; 920 AA.
AC D7TGM4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN OrderedLocusNames=VIT_12s0035g01740 {ECO:0000313|EMBL:CBI29646.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI29646.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595990; CBI29646.3; -; Genomic_DNA.
DR RefSeq; XP_002268311.1; XM_002268275.3.
DR AlphaFoldDB; D7TGM4; -.
DR STRING; 29760.D7TGM4; -.
DR PaxDb; 29760-VIT_12s0035g01740-t01; -.
DR EnsemblPlants; Vitvi12g02111_t001; Vitvi12g02111_P001; Vitvi12g02111.
DR GeneID; 100245514; -.
DR Gramene; Vitvi12g02111_t001; Vitvi12g02111_P001; Vitvi12g02111.
DR KEGG; vvi:100245514; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_016157_1_0_1; -.
DR InParanoid; D7TGM4; -.
DR OMA; KMVRKPI; -.
DR OrthoDB; 1209347at2759; -.
DR Proteomes; UP000009183; Chromosome 12.
DR ExpressionAtlas; D7TGM4; baseline and differential.
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; 2.
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:SF230; 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; 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:UP000009183}.
FT DOMAIN 36..306
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 575..698
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 734..827
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 504..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 100128 MW; 057D023723D9DC7D CRC64;
MEAIDELVQL SDSMRQAAAL LADEDVDESA SSSKRPSTFL NVVALGNVGA GKSAVLNSLI
GHPVLPTGEN GATRAPISID LNRDASVSSR SIILQIDNKS QQVSASALRH SLQDRLSKSS
SGKSRDEIYL KLRTSTAPPL KLIDLPGLDQ RIVDDSMISG YVQHNDAILL VITPAAQAPE
ISSSRALRIA KEYDADSTRT IGVISKIDQA AGEPKILAAV QALLSNQGPR STSDIPWVAL
IGQSVSIASA QSGNAGSENS LETAWRAESE TLKSILPGAP QNKLGRVALV DALAQQIRNR
MKVRLPNLLS GLQGKSQIVQ EELVRLGEQM VDSVEGTRAI ALQLCREFED KFLQHLAHGE
GSGWKVVASF EGNFPNRIKQ LPLDKHFDIN NVKRIVLEAD GYQPYLISPE KGLRSLIKIV
LELAKEPSRL CVDEVHRVLV DIVSAAANAT PGLGRYPPFK REVVAIASTA LEGFKNEAKK
MVVALVDMER AFVPPQHFIR LVQRRMDRQR REEEVKNRSS KKGLDAEQSI LNRATSPQTG
GQQTGGSLKT MKDKSSQQDK EGQEGPALKT AGPGGEITAG FLLKRSAKTN GWSRRWFVLN
EKSSKLGYTK KQEERHFRGV INLEECNIEE IADEDEPPPK SSKSKKENGP EKSPSLVFKI
TSKVPYKTVL KAHSAVVLKA ESAVDKAEWL NKLRNVIQPS GQVKGESGLT MRQSLSDGSL
DTMARRPADP EEELRWMSQE VRGYVEAVLN SLAANVPKAV VLCQVEKSKE DMLNQLYSSV
SAQSTARIEE LLQEDQNVKR RRERNQKQSS LLAKLTKQLS IHDNRAAAAS SSWSNGGAES
SPRTPGPSSG DDWRSAFDAA ANGPTDSYSN SSRSGANGHS RRYSDPSQNG DANSGPNSGS
RRTPNRLPPA PPQSGSSYRY
//