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Database: UniProt
Entry: G2Y7N0_BOTF4
LinkDB: G2Y7N0_BOTF4
Original site: G2Y7N0_BOTF4 
ID   G2Y7N0_BOTF4            Unreviewed;       812 AA.
AC   G2Y7N0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Similar to dynamin protein dnm1 {ECO:0000313|EMBL:CCD48632.1};
GN   ORFNames=BofuT4_P110160.1 {ECO:0000313|EMBL:CCD48632.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD48632.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790293; CCD48632.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2Y7N0; -.
DR   STRING; 999810.G2Y7N0; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   InParanoid; G2Y7N0; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; 1.20.120.1240; Dynamin, middle domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 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   SMART; SM00302; GED; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT   DOMAIN          27..311
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          724..812
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          535..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  90146 MW;  F7C19D555F0C525E CRC64;
     MAALGEDLLG IVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINVPSEEE DAPEAHTAAS VATQPEWAEF HHIPNRRFTE FQDVKREIEN
     ETARIAGNNK GINRSPINLK IYSPHVLSLT LVDLPGLTKV PIGDQPTDIE KQTRNLISEY
     IAKPNSIILA VSPANVDIVN SEALKLARHV DPLGRRTIGV LTKIDLMDHG TNAMDILSGR
     VYPLKLGFIG VVNRSQQDIQ GNKTLSEALK SEADFFKHHP AYRNMATRCG TQFLAKSLNT
     TLMAHIRERL PDIKARLNTL MGQTQQELAS YGDMHFSGKE HKGALILQLM TRFASSFIAS
     IDGTSTEIST KELCGGARIY YIFNSVFGNS LETIDPTTNL SALDIRTAIR NSTGPRPSLF
     VPELAFDLLV KPQIKLLEVP SQRCVELVYE ELIKICHTCG STELTRFPRL QTKLIEVVSD
     LLRERLGPAS QYVESLISIQ RAYINTNHPN FLGAAAAMSN VVSNKQEKER RRLIQEEKER
     KEHRRRKELE AANGGETPEE EADAVPEKLE NLPHRKHLQK TSRSMSPAIR ENGTSAMVSS
     MNGLRGGSPP RFNGQAAGGA RDSFLNYFFG KDGGLPGGAG VPQASSSAQM MGNPNLGRHV
     SQSAEPSITQ SIRRQEERPV QRTPAQQARE DDYELGRAQR DYNYDSPFGN NAEPALTDRE
     AMETELIRAL ISSYFNIVRE SIADQVPKAV MHLLVNHSKD VVQNRLVSEL YREDLFGELL
     YEDDAVKKER EKCEKLLRTY KEAAKIVGEV GI
//
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