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Database: UniProt
Entry: L8G1G1_PSED2
LinkDB: L8G1G1_PSED2
Original site: L8G1G1_PSED2 
ID   L8G1G1_PSED2            Unreviewed;       806 AA.
AC   L8G1G1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   22-FEB-2023, entry version 48.
DE   SubName: Full=Dynamin GTPase {ECO:0000313|EMBL:ELR06982.1};
GN   ORFNames=GMDG_08216 {ECO:0000313|EMBL:ELR06982.1};
OS   Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS   white-nose syndrome fungus) (Geomyces destructans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR06982.1, ECO:0000313|Proteomes:UP000011064};
RN   [1] {ECO:0000313|Proteomes:UP000011064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Geomyces destructans 20631-21.";
RL   Submitted (SEP-2010) 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}.
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DR   EMBL; GL573484; ELR06982.1; -; Genomic_DNA.
DR   RefSeq; XP_012746676.1; XM_012891222.1.
DR   AlphaFoldDB; L8G1G1; -.
DR   STRING; 658429.L8G1G1; -.
DR   VEuPathDB; FungiDB:GMDG_08216; -.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   InParanoid; L8G1G1; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000011064; 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; 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:UP000011064}.
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..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..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   806 AA;  89626 MW;  BF6AD1167A450E27 CRC64;
     MASLGENLLG IVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINVPSDND APEGSEVYEP HTPASVEAQG EWGEFHHIPG RQFTNFQDVK
     REIENETARI AGNNKGINRS PINLKIYSPH VLSLTLVDLP GLTKVPIGDQ PSDIEKQTRN
     LISEYIAKPN SIILAVSPAN VDIVNSEALK LARHVDPLGR RTIGVLTKID LMDHGTNALD
     ILSGRVYPLK LGFIGVVNRS QQDIQGNKTL AEALKSESDF FRHHPAYRNM ANRCGTQFLA
     KSLNTTLMSH IRERLPDIKA RLNTLMGQTQ QELASYGDMH FNGKEHRGSL ILQLMTRFAS
     SFISSIDGTS TEISTKELCG GARIYYIFNS VFGNSLETID PTTNLSALDI RTAIRNSTGP
     RPSLFVPELA FDLLVKPQIK LLEIPSQRCV ELVYEELIKI CHTCGSTELT RFPRLQGKLI
     EVVSDLLRER LGPASNYVES LISIQRAYIN TNHPNFLGAA AAMSHVVTKK QENEKKKLLQ
     EERERREKRR QKELGAANGV DGAEDEDEVS EKAEGLPHRS KMHKSGRSTS PHVRQNGTSA
     SIAERINGQR ASSPTRFGTQ ANPKDSFLNY FFGKDGAPGG GPGVGQAASS AQNPNLGRHV
     SQSTEPSITQ SIRRQEERNT HRSPAQQTRD EDYAREYDYS SPFGNNTEPA LTDREAMETE
     LIRALISSYF DIVRESIADQ VPKAVMHLLV NHSKDVVQNR LVSELYREDM FEELLYEDDA
     VKKEREKCER LLKTYREAAK IVGEVL
//
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