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Database: UniProt
Entry: A0A094AWW4_9PEZI
LinkDB: A0A094AWW4_9PEZI
Original site: A0A094AWW4_9PEZI 
ID   A0A094AWW4_9PEZI        Unreviewed;       806 AA.
AC   A0A094AWW4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Dynamin GTPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V494_07266 {ECO:0000313|EMBL:KFY33849.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY33849.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY33849.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY33849.1}.
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DR   EMBL; JPJW01002311; KFY33849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AWW4; -.
DR   STRING; 1420907.A0A094AWW4; -.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000029288; 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:UP000029288}.
FT   DOMAIN          27..316
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          719..806
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          527..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  89620 MW;  CFA2E885CEEBCA9E CRC64;
     MASLGENLLG IVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINVPSDND APEGSDVHVP HTPASVEAQG EWGEFHHIPG RQFTNFQDVK
     REIENETARI AGNNKGINRS PINLKIYSPH VLSLTLVDLP GLTKVPIGDQ PSDIEKQTRN
     LISEYIAKPN SIILAVSPAN VDIVNSEALK LARHVDPLGR RTIGVLTKID LMDHGTNAMD
     ILSGRVYPLK LGFIGVVNRS QQDIQGNKTL AEALKSESDF FKHHPAYRNM ANRCGTQFLA
     KSLNTTLMAH IRERLPDIKA RLNTLMGQTQ QELASYGDMH FNGKEHRGSL ILQLMTRFAS
     SFISSIDGTS TEISTKELCG GARIYYIFNS VFGNSLETID PTTNLSALDI RTAIRNSTGP
     RPSLFVPELA FDLLVKPQIK LLEIPSQRCV ELVYEELIKI CHTCGSTELT RFPRLQGKLI
     EVVSDLLRER LGPASNYVES LISIQRAYIN TNHPNFLGAA AAMSHVVTKK QENEKKKLLQ
     EERERREKRR QKELAATNGV DGHEEEDEAT EKAEGLPHRS KVHKSGRSTS PHVRQNGTSS
     IAERINGQRA SSPTRFGAQG NNPKDSFLNY FFGKDGAPGS APGVGHSASS AQNPNLGRHV
     SQSAEPSITQ SIRRQEERNT HRSPAQQTRD EDYAREYDYS SPFGDSTEPA LTDREAMETE
     LIRALISSYF DIVRESIADQ VPKAVMHLLV NHSKDVVQNR LVSELYREDM FEELLYEDDA
     VKKEREKCER LLKTYREAAK IVGEVL
//
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