ID A0A162JGX8_9HYPO Unreviewed; 903 AA.
AC A0A162JGX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Dynamin, GTPase domain protein {ECO:0000313|EMBL:OAA41893.1};
GN ORFNames=BBO_05252 {ECO:0000313|EMBL:OAA41893.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41893.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41893.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41893.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA41893.1}.
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DR EMBL; AZHA01000015; OAA41893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162JGX8; -.
DR OrthoDB; 5491472at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
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 PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF149; GTPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G11890)-RELATED; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 4: Predicted;
FT DOMAIN 36..317
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 619..710
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 699..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 99940 MW; 96A1AD68D164BB21 CRC64;
MAGLYSAAAL NELNSPEAEV LHNLMAKLSS CGVGDIVDIP QMIVVGQQAV GKSSVLEAIS
RVKFPTAAGL CTRFATEIIL GRAQEESVNV TIRFHKSEPQ PAGTFDESGL SKDDLPALVE
QAKKYMGITE NTTGFSRHVL CVQIRGPDIL PLRLVDLPGI FNNEIATQSE KGIEIVNQLV
ESYMEHKNSI ILVVVEAKTA VVNHYALAKV KDFDPKRERT LGIITKPDLK LGEHLQREHI
QLAKNREPKH TLKLGWHVLR NRAEDEDEEG TETRDEIEDA FFKTSPWNSI VEEDRGIHSL
RQKLSTVLYN HIRRGLPKVI QDIETNLAKR QTERGQLGVE RPKLEDKRVF LADIAEQFQR
LVRDAMKGNY ADQFFGQLTE PLHRLRADLK CFHRAFDYTL TTRGHNFEIA PFGDGDEEEN
QVDSVPEALV DFLARNPYDF ALPTKTSRKD INDLLVKPVV ASEGSELPGT CNSEVAVHLF
QLQSARWDKI ARFHVEYVTQ YAKFFIEQLF VHIIGQDSEH RDVILSEYVD PFFEKHETML
KVKLDELVAP YANGYAAPAE AEFRQMVSGW TVDRVVQRLR NIEHSVEDED RDGSRRIRHD
FVSAAEELAQ IVDGGSLGTE RIVNMMQAYY EISRRTFLDN VTNLAVEGCL IQQLPSIFTS
KQIAAMDEST INKLASESGN VQSRRDQLSQ EIESLKTGLE QCRRWRPRTE LENPTRPNDT
SGADPLGKNG HESRPAQKKD ALSRGATPAA NNFGTMLRDQ SAKVANTFPW GSTTESNATT
HSNLPGRKPA TLNKNPSLQK LSSQSFNFAS TAQTSSTGLF GSKPTALNSN SSSSSSSVFG
NTPTQTAPFG GVDSTIDGPF GKKPQANNST APSFPAFGGG NRVSGLFSGS TTKPGAGGPG
AQV
//