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Database: UniProt
Entry: Q2HG88_CHAGB
LinkDB: Q2HG88_CHAGB
Original site: Q2HG88_CHAGB 
ID   Q2HG88_CHAGB            Unreviewed;       789 AA.
AC   Q2HG88;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ92531.1};
GN   ORFNames=CHGG_00766 {ECO:0000313|EMBL:EAQ92531.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92531.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92531.1; -; Genomic_DNA.
DR   RefSeq; XP_001219987.1; XM_001219986.1.
DR   AlphaFoldDB; Q2HG88; -.
DR   STRING; 306901.Q2HG88; -.
DR   GeneID; 4386871; -.
DR   VEuPathDB; FungiDB:CHGG_00766; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   InParanoid; Q2HG88; -.
DR   OMA; KICHNCG; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000001056; 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:UP000001056}.
FT   DOMAIN          27..300
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          702..789
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          526..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  87134 MW;  D54BFFE4295BA56C CRC64;
     MAALGDDLLG TVNKLQDLVF NTIGNDSLDL PQIVVVGSQS AGKSSVLENI VGRDFLPRGS
     GIVTRRPLIL QLINVPGDDA GEDPHAGYRN PSQAAPNEWA EFHHIPNRRF NDFGDVKREI
     ENETSRVAGN NKGINRQAIN LKIFSPNVLN LTLVDLPGLT KTRNLISEYI AKPNSIVLAV
     SPANVDIVNS EALKLARHVD PLGRRTIGVL TKVDLMDHGT NALEILSGRV YPLKLGWIGV
     VNRSQQDIQG NKPMEDALKS ESEFFRHHPA YRNISTRCGT RFLAKTLNTT LMAHIRDRLP
     DIKARLNTLM GQTQQELASY GDMHFSGKEH RGSLILQLMT RFASSFISSI DGTSTEISTK
     ELCGGARIYY IFNSVFGSSL ESIDPTSNLS ALDIRTAIRN STGPRPSLFV PEMAFDLLVK
     PQIKLLEVPS QRCVELVYEE LIKICHTCGS TELSRFPRMQ AKLIEVVSDL LRERLGPASG
     YVESLISIQR AYINTNHPNF LGAAAAMSHV VSNKQERERK RLIQEERERR ERRRMKELGA
     NGADTPVDEE DEHAATEKLD SVAARKALGK TGRSHSPSVR DSSSGGIAAA LNGVRSSSPA
     QFNGQGLGTA KDSFLNYFFG KDGAIVPGTP PATSNLGRHV SQSVEPTFSQ SMRRPEDKPL
     RSPPPPPIRV DDAALDFAGG SKGNDFMNGS EPAMTDREAM ETELIRALIS SYFNIVRESI
     ADQVPKAIMH LLVNHCKDVV QNRLVTELYK EALFEELLYE DDAVKKDREK CERMLQTYRE
     ASKIIGEVV
//
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