ID A0A059B8N4_EUCGR Unreviewed; 923 AA.
AC A0A059B8N4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN ORFNames=EUGRSUZ_G00082 {ECO:0000313|EMBL:KCW62592.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW62592.1};
RN [1] {ECO:0000313|EMBL:KCW62592.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW62592.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198759; KCW62592.1; -; Genomic_DNA.
DR RefSeq; XP_010065245.1; XM_010066943.2.
DR AlphaFoldDB; A0A059B8N4; -.
DR STRING; 71139.A0A059B8N4; -.
DR EnsemblPlants; KCW62592; KCW62592; EUGRSUZ_G00082.
DR GeneID; 104452468; -.
DR Gramene; KCW62592; KCW62592; EUGRSUZ_G00082.
DR KEGG; egr:104452468; -.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; A0A059B8N4; -.
DR OrthoDB; 1209347at2759; -.
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 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:SF238; DYNAMIN-2B; 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}.
FT DOMAIN 39..309
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 579..704
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 742..835
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 509..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 100266 MW; CD9297AF58467148 CRC64;
MEAIEELVQL SDSIRQASAL LADEDVDESS SSSSSSKRAT TFLNVVALGN IGAGKSAVLN
SLIGHAVLPT GEGGATRAPI SIDLNRDSSL STKSIVLQID SKSQQVSASA LRHSLQDRLS
KGSSGRSRDE IYLKLRTSTA PPLKLIDLPG LDQRVMDDSL ISEYIQHNDA ILLVVVPATQ
VLEISSSRAL KAAKEYDSES TRTVGVISKI DQAASDSRAL AAVQALLLNK GPPRTADIPW
VALIGQSVSI ASAQSGGVGS ENSLETAWRA ESESLKSILT GAPQSKLGRV ALVDALAAQI
RNRMKLRVPN LLSGLQGKSQ IVQDELVRLG EQMVNSPEGT RALALELCRE FEDKFLLHIT
GGEGSGWKIV ASFEGNFPNR IKQLPLDRHF DINNVKRIVL EADGYQPYLI SPEKGLRSLI
KSVLEMAKEP SRLCVDEVHR VLMDIVSAAA TATPGLGRYP PFKREVITIA TAALETFKNE
AKKMVVALVD MERAFVPPQH FIRLVQRRME RQRREDELKN RSSKRGVADA EQSTLNRATS
PQTGGQQSGG SLKSMKEKPN QQDKDGPEGS VLKTAGPDGE MTAGFLLKKS AKTNGWSKRW
FVLNEKTGKF SYTRKPEERL FRGTIILQEC NLEEISDDDE PPPKSSKDKK SNGPDSGKGP
GLIFKITSKV PYKTVLKAHS AVVLKAETMA EKVEWLNKLR NVVPPSAGGQ MKGESGLPLR
QSLSDGSLDT MARRPADPEE ELRWMSQEVR GYVEAVLNSL GANVPKAVVL CQVEKAKEDM
LNQLYSSISA QSTARIEELL LEDHNVKRKR EKCQKQASLL SKLTRQLSIH DNRASAASSW
SDSSSAAESP RSNGPSSGDD WRSAFDAASN GHSDSSRFGT SHSRRKSDPA QNGDVSPASN
PGGRRTPIRL PPAPPQSGST YRY
//
