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Database: UniProt
Entry: A0A078I907_BRANA
LinkDB: A0A078I907_BRANA
Original site: A0A078I907_BRANA 
ID   A0A078I907_BRANA        Unreviewed;       920 AA.
AC   A0A078I907;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=BnaC01g28250D {ECO:0000313|EMBL:CDY45889.1};
GN   ORFNames=GSBRNA2T00082867001 {ECO:0000313|EMBL:CDY45889.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY45889.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY45889.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
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; LK032640; CDY45889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078I907; -.
DR   STRING; 3708.A0A078I907; -.
DR   PaxDb; 3708-A0A078I907; -.
DR   EnsemblPlants; CDY45889; CDY45889; GSBRNA2T00082867001.
DR   Gramene; CDY45889; CDY45889; GSBRNA2T00082867001.
DR   OMA; KYVERND; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
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: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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000028999}.
FT   DOMAIN          35..303
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          578..702
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          736..829
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          507..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..656
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   COILED          790..820
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        521..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..903
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  100000 MW;  86659F89F9CD9B3C CRC64;
     MAAIDELSQL SDSMRQAAAL LADEDPDESS SSRRPATSLN VVALGNVGAG KSAVLNSLIG
     HPVLPTGENG ATRAPIIIDL SREESLSSKA IILQIDNKSQ QVSASALRHS LQDRLSKGAT
     GRGRDEIYLK LRTSTAPPLK LIDLPGLDQR IVDDSMIGEH AQHNDAILLV VVPASQASEI
     SSSRALKIAK EYDSDSTRTV GIISKIDQAA ENPKALAAVQ ALLSNQGPPK TTDIPWVALI
     GQSVAIASAQ SGGSENSLET AWRAESESLK SILTGAPQSK LGRIALVDTL ASQIRSRMKL
     RLPNILSGLQ GKSQIVQDEL SRLGEQLVSS AEGTKAIALE LCREFEDKFL LHLTGGEGSG
     WKVVASFEGN FPNRIKQLPL DRYFDLNNVK RIVLEADGYQ PYLISPEKGL RSLIKIVLEL
     AKDPARLCVD EVHRVLVDIV SASANATPGL GRYPPFKREV VAIASAALDG FKNEAKKMVV
     ALVDMERAFV PPQHFIRLVQ RRMERQRRED ELKGRSSRKG QDAEQSLLNR ASSPQPEGSS
     TGGSLKSLKD KFLPQDKDKD KDKETPEVSG LKTAGPEGEI TAGYLLKKSA KTNGWSRRWF
     VLNEKTGKLG YTKKQEERNF RGTVTLEECS IEEISDDEGE KSKSSKDKKS NGPDSKGPGL
     VFKITCRVPY KTVLKAHNAL VLKAESMVDK NEWINKLQKV IQARGGQVGG ASMRQSLSEG
     SLDKMVRKPV DPEEELRWMS QEVRGYVEAV LNSLAANVPK AVVLCQVEKS KEDMLNQLYS
     SISAIGNERI ESLIQEDQNV KRKRDRYEKQ SSLLSKLTRQ LSIHDNRAAA ASSWSDSGTE
     SSPKTNGGST GEDWMNAFNA AASGPDSLKR YGSGGHSRRY SDPAQNGEDD SSGSGGSNRR
     TTPNRLPPAP PQSGGSSYRY
//
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