ID A0A0D9X7Z6_9ORYZ Unreviewed; 886 AA.
AC A0A0D9X7Z6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR08G12490.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR08G12490.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR08G12490.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR08G12490.1}
RP IDENTIFICATION.
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; A0A0D9X7Z6; -.
DR STRING; 77586.A0A0D9X7Z6; -.
DR EnsemblPlants; LPERR08G12490.1; LPERR08G12490.1; LPERR08G12490.
DR Gramene; LPERR08G12490.1; LPERR08G12490.1; LPERR08G12490.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_016157_1_0_1; -.
DR Proteomes; UP000032180; Chromosome 8.
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:UP000032180}.
FT DOMAIN 37..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..825
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..121
FT /note="Polar residues"
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 826..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 96638 MW; 18AA8F07BFF9AC48 CRC64;
MEAIEELSEL ADATRQASSL LADDDPSEPR AQRRGGGSSF LTVVALGNIG AGKSAVLNGL
IGHPVLPTGE NGATRAPICV DLQRDASLST KSIMLQVDSK SQQVSASSLR HSLQDRLSKA
NGSGKGRSDE INVKLSTSTA PALKLFDLPG IDQRSMDESM IGNYAARSDA ILLVIIPALQ
APDVASSRAL RIARELDSEG SRTIGVLSKV DQVAADQKAL GAVQALLVNQ GPRTAADIQW
IATIGNSVPI ASVQSGVGSE TSPDTRQAEV ESLISILVGS PQSKLGREAL VDSLAKQIRA
RMKVRLPNLL NGLEGKSQII QEELAKLGEQ MVQSSEGTRV IALGLCREFE DKFLQHITGV
EGAGWKVVAS FEGKFPTRIK QLPLDKHFDM KNVKRIVLEA DGYQPYLISP EKGLRSLIRG
LLELAKEPST LLVDEVHRVL LDIVSATANA TPGLGRYPPF KREVIAIASA ALDGFKDEAK
KMVTALVDME RAFVPPQHFI RLLQRRMERQ RHEDELKSRS TKKASDGDSS KATSPQAQTK
EGSNLQVLGP AGEITAGFLL KKRAKANDWS KRWFVLNEKS GKLGYTKKQE ERHFRGVINL
EECNFEEILD EEDPLRSSKD SKKANVPDFG TPGLSFKITH KIAYKNVLKA HKAIILKAES
MADKTEWVNK IKSIVDQKGA SAKSSLPMRQ SHSDGSLMSN SKKDASLDTI LRKPVDPEED
LKWISQEVRG YVEAVLSSLA ANIPKLSIRC LVEAFLAVVL CQVEKAKEDM LNQLYTSISM
RSIDRIEELI QEDHNVKHRR EKFKMQSSLL SKVTRLLRIH DNRSASANWT NDSAGSESSP
RSSGHSGDEW KSAFDPSQDV DSSAGTNSGS RRIPSRMPPP PPPKGG
//
