GenomeNet

Database: UniProt
Entry: A0A0D2CF53_9EURO
LinkDB: A0A0D2CF53_9EURO
Original site: A0A0D2CF53_9EURO 
ID   A0A0D2CF53_9EURO        Unreviewed;       806 AA.
AC   A0A0D2CF53;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Dynamin GTPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV07_12110 {ECO:0000313|EMBL:KIW22199.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22199.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW22199.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22199.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN847047; KIW22199.1; -; Genomic_DNA.
DR   RefSeq; XP_016242415.1; XM_016399603.1.
DR   AlphaFoldDB; A0A0D2CF53; -.
DR   STRING; 569365.A0A0D2CF53; -.
DR   GeneID; 27351304; -.
DR   VEuPathDB; FungiDB:PV07_12110; -.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000054466; 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:UP000054466}.
FT   DOMAIN          27..319
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          536..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  89093 MW;  B4161BA29F138E6F CRC64;
     MTTLGDDLLR TVNKLQDLVF NTIGNDSLDL PQIVVVGSQS SGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINIPPEDD DSDTNGNGDV HVPHTAASVA EHGEWAEFHH IPGRKFTDFN
     QVRAEIENET ARIAGNNKGI NRQPINLKIF SPHVLNLTLV DLPGLTKVPI GDQPSDIEKQ
     TRTLISEYIA KPNSIILAVS PANVDIVNSE ALKLARHVDP MGRRTIGVLT KLDLMDHGTN
     ALDILSGRVY PLKLGFIGVV NRSQQDIQTN KPMSEALRSE AEFFRHHPAY RNMATRCGTQ
     YLAKTLNTTL MGHIRDRLPD IKARLNTLMG QTQQELASYG SKQFSGKEHR GSLILQLMTR
     FATSFISSID GTSSEISTKE LCGGARIYYI FNSVFGNSLE TIDPTHNLSV LDIRTAIRNS
     TGPRPSLFVP ELAFDLLVKP QIKLLEIPSQ RCVELVYEEL IKICHTCGST ELSRFPRLQG
     KLIEVVSDLL RERLGPCSNY VESLIAIQRA YINTNHPNFL GAAAAMSSVI ASKNEKDKKL
     AQAEERRKRE KQRMKQLGVN GAATPDEEDA EQEDKPTSLP NRKHPTLSRS MSPAVTRERE
     NGIGSISAAA GSAGAARDSF LNYFFGKEGG LPGASLQGSP AVVPSSASVA QRHVSHSVDP
     SFAQSMRRMD RGSFTDRSPV YPPALHDDYA PGSEYGDSSL LFPEQNAEPA LTEREALETE
     LIRRLISSYF NIVRETIADQ VPKAIMHLLV NHSRDEVQNR LVSELYKEDL FGELLYEDDG
     IKKEREKCEK LLATYKEAAK IVGEVL
//
DBGET integrated database retrieval system