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Database: UniProt
Entry: D7TGM4_VITVI
LinkDB: D7TGM4_VITVI
Original site: D7TGM4_VITVI 
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
//
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