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Database: UniProt
Entry: A0A0E0IC20_ORYNI
LinkDB: A0A0E0IC20_ORYNI
Original site: A0A0E0IC20_ORYNI 
ID   A0A0E0IC20_ORYNI        Unreviewed;       869 AA.
AC   A0A0E0IC20;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA08G16310.2};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA08G16310.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA08G16310.2};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA08G16310.2}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA08G16310.2};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0IC20; -.
DR   EnsemblPlants; ONIVA08G16310.2; ONIVA08G16310.2; ONIVA08G16310.
DR   Gramene; ONIVA08G16310.2; ONIVA08G16310.2; ONIVA08G16310.
DR   HOGENOM; CLU_016157_1_0_1; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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:SF233; 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:UP000006591}.
FT   DOMAIN          36..307
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          552..676
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          721..808
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          510..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  94909 MW;  438CAD5356127B21 CRC64;
     MEAIEELSEL ADATRQASAL LADDDPSELP AQRRGGSSFL TVVALGNIGA GKSAVLNGLI
     GHPVLPTGEN GATRAPICVD LQRDASLSSK SIMLQIDSKS QQVSASSLRH SLQDRLTKAG
     SFGKGRSEEI NVKLCTSTAP PLKLIDLPGI DQRSMDESMI GNYAARNDAI LLVIVPALQA
     PDVASSRALR IARELDSEGS RTIGVVSKVD QVAEDQRALL AVQALLVNQG PRTAADIQWI
     ATIGNSVPIA SVQSGVGSES SPETIWKVEV ESLKSILLGS PQSKLGREAL VDSLAKQIRT
     RIKVRLPNIL NGLQGKSQII QEELAKLGEQ MVQSSEGTRV IALGLCREFE DKFLQHITGV
     EGGGWKVVAS FEGKFPTRIK QLPLDKHFDM KNVKRIVLEA DGYQPYLISP EKGLRSLIKG
     LLELAKEPSI LLVDEVHRVL LDIVSATANA TPGLGRYPPF KREVIAIGSA ALDGFKDEAK
     KMVIALVDME RAFVPPQHFI RLLQRRMERQ RHEDELKSRS TKKVSDAEPS KATSPQTQTK
     EGSNLQVLGP AGEITAGFLF KKRAKANDWS NRWFVLNERS GKLGYTKKQE ERHFRGVINL
     EECNLEEVLD EEDPTRSLKD PKKPNVPDIG TPGLIFKITH KVAYKNVLKA HKAIILKAES
     MAEKTEWVTK IRSIVDQKGA SATSGLPMRQ SHSDGSLMST SKKDGSLDTM LRKPVDPEEE
     LKWISQEVRG YVEAVLSSLA ANAVVLCQVE KAKEDMLNQL YTSISVERIE ELIQEDHSVK
     HRREKIKKQS SLLSKVTRLL RIHDNRSATS NWSNDSAGSD SNPGSSGQSG DEWKSAFDPS
     QDVDPSAAGT NTGSRRIPSR MPPPPPQGG
//
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