ID   A0A164TJ11_9AGAM        Unreviewed;       924 AA.
AC   A0A164TJ11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dynamin GTPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SISNIDRAFT_442155 {ECO:0000313|EMBL:KZS92405.1};
OS   Sistotremastrum niveocremeum HHB9708.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS92405.1, ECO:0000313|Proteomes:UP000076722};
RN   [1] {ECO:0000313|EMBL:KZS92405.1, ECO:0000313|Proteomes:UP000076722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB9708 {ECO:0000313|EMBL:KZS92405.1,
RC   ECO:0000313|Proteomes:UP000076722};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV419410; KZS92405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164TJ11; -.
DR   STRING; 1314777.A0A164TJ11; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000076722; Unassembled WGS sequence.
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; 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; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 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:UP000076722}.
FT   DOMAIN          238..510
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          814..907
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          155..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   924 AA;  103510 MW;  A9C5F19D9B7C7F70 CRC64;
     MLRSAPKKLK VQLDKASTAQ QRVVHRRFTT FSSSSTTSTR FRFRNSAPWA ASLRHIHARA
     ISYSSIPKFV ARAFRVPVAG ATVGAGAFGY ANYKVEELRT KSKEWINAAQ ESAGDFIDSA
     SDAFKSAQSK LASIEIPTVE TPQFVKDLFA SLSSNSEGRK SNDGGNGHES GRGGPGDEEK
     ATIAALLAAT LSGPSTDAPS NNESRSEDPD SRQNDLMRMT RKLIEIRSIL LSIDQSDSLK
     LPSIVVIGSQ SSGKSSVLEA IVGHEFLPKG NNMVTRRPIE LTLIHTPRKS GLDAEEYGEF
     PALGLGKITN FSQIQQTLTD LNLAVPASEA VSNDPIDLRI YSPYVPDLTL IDLPGYVQIA
     SMDQPETLKE KVAALCDRYI REPNIILAVC AADVDLANSP ALRASRKVDP LGLRTIGVVT
     KMDLVQPEQG VSILSNNRYP LHLGYVGVVC KPSKKDSHES PRTVARRGED SYFGSHKDYF
     GSSSSLMVGT ETLRRRLMEV LESSMASSLH GITNAVQLEL EEATYQFKVQ FNDRRISAES
     YVAETVDSLK ARFRDFTSQF TKPHIRAKLK AMLDEKSMDV LEQLYWSDKR SEELTALATD
     VKVKPETVDS YWRYKLDAAS SLLTKSGVGR DSTILVADGL RSLMETIASG EPFNYHPRAA
     ERLIQFSHMI LRDRIGVASD QVENCIKPYK YEIEVDAREW EDGRVNAIEL SEREIQMCEG
     KLKEIKKRVG GGRYLNRLIA YVKLLEDQET DKKRLRRSQD EDAQDDAPNP LIDNYRYNPA
     HVLDARHAML YSDRLNILKL RAAALKSKRC KGGPQNDVFC PEAFLNVVST KLAYTAAMFI
     NIELLDQFFY QFPREIDSRL IYDQDRNEIL EFARENPVIR KHLDLQERKD KLEEVMKQLQ
     SLSHFRKDSQ PAPRRQRGLF GGMF
//