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Database: UniProt
Entry: A0A218YTG9_9HELO
LinkDB: A0A218YTG9_9HELO
Original site: A0A218YTG9_9HELO 
ID   A0A218YTG9_9HELO        Unreviewed;       827 AA.
AC   A0A218YTG9;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OWO98555.1};
GN   ORFNames=B2J93_2873 {ECO:0000313|EMBL:OWO98555.1};
OS   Marssonina coronariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=503106 {ECO:0000313|EMBL:OWO98555.1, ECO:0000313|Proteomes:UP000242519};
RN   [1] {ECO:0000313|EMBL:OWO98555.1, ECO:0000313|Proteomes:UP000242519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:OWO98555.1,
RC   ECO:0000313|Proteomes:UP000242519};
RA   Cheng Q.;
RT   "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT   blotch.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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:OWO98555.1}.
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DR   EMBL; MZNU01000389; OWO98555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218YTG9; -.
DR   STRING; 503106.A0A218YTG9; -.
DR   InParanoid; A0A218YTG9; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000242519; Unassembled WGS sequence.
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:UP000242519}.
FT   DOMAIN          27..311
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          739..827
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          523..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  91862 MW;  75E6B8E1ED5D28C7 CRC64;
     MAALGEDLLG IVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINIPTDEE DAPEEHSAAA VATQPEWAEF HHIPNRRFTE FQDVKREIEN
     ETSRIAGNNK GINRSPINLK IYSPHVLSLT LVDLPGLTKV PIGDQPTDIE KQTRNLISEY
     IAKPNSIILA VSPANVDIVN SEALKLARHV DPLGRRTIGV LTKVDLMDHG TNALDILSGR
     VYPLKLGFIG VVNRSQQDIQ GNKSLAEALK SESDFFKHHP AYRNMSNRCG TQFLAKSLNT
     TLMAHIRERL PDIKARLNTL MGQTQQELAS YGDMHFSGKE HRGSLVLQLM TRFASSFISS
     IDGTSTEIST KELCGGARIY YIFNSVFGNS LETIDPTTNL SALDIRTAIR NSTGPRPSLF
     VPELAFDLLV KPQIKLLEVP SQRCVELVYE ELIKICHTCG STELTRFPRL QAKLIEVVSD
     LLRERLGPSS SYVESLISIQ RAYINTNHPN FLGAAAAMSN VVTNKQERER KRLIQEERER
     RERRRQKELG ANGADSPEDQ EETEEKNENL LQRKALHKGA RSLSPVVREN GSGGIAATMN
     GTRSGSPPRF NGQAAGGARD SFLNYFFGKD GGLPAGGASA GQGPSSVQNP NLGRHVSQSA
     EPSFSQSIRR QEERQVHRTP AQQLREDDYE LGRSQRDYDY NSPFVGSQNL ALSYMENANG
     VIQGNNNEPA LTDREAMETE LIRALISSYF NIVRESIADQ VPKAVMHLLV NHSKDVVQNR
     LVSELYREDL FEELLYEDDA VKKEREKCEK LLKTYREAAK IVGEVGI
//
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