ID   G3YH31_ASPNA            Unreviewed;       919 AA.
AC   G3YH31;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Mitochondrial dynamin GTPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPNIDRAFT_52714 {ECO:0000313|EMBL:EHA18035.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA18035.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA18035.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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:EHA18035.1}.
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DR   EMBL; ACJE01000021; EHA18035.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3YH31; -.
DR   STRING; 380704.G3YH31; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1160709; -.
DR   HOGENOM; CLU_008640_0_0_1; -.
DR   Proteomes; UP000009038; 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}.
FT   DOMAIN          236..509
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          801..894
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          157..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..910
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  102065 MW;  D9F6032EF8BED969 CRC64;
     MSGRILSHRL VPLLRTGLLA RHVHNAAART GGLLRSDGSA ALRGRAWPVG ANAIHNNVPA
     VRAISFHRIL PKLAIKLIRL PAMLGGATVA GLAYFQYQAT QAGNYAIDLF KRAGETAGDA
     ASSLFTEIQG IAEQTQRGWQ RTTDAVELPE WLQNFINPNE ESQSDNGGPG GKRPKESRLG
     AAAAGATTAG AFGYDESNEE DTRSERKIAE DDQMMLLTRK MIEIRNILQT VGQSNTLTLP
     SIVVIGSQSS GKSSVLEAIV GHEFLPKGTN MVTRRPIELT LVNTPNAQAE YGEFPALGLG
     KITDFSQIQR TLTDLNLAVP ERDCVSDDPI QLSIYSPHVP DLSLIDLPGY IQVAGHDQPP
     ELKQKISDLC DKYIQAPNVI LAISAADVDL ANSTALRASR RVDPRGERTI GVITKMDLVD
     PERGYNVLSD KKYPLRLGYV GVVSRIPQTT ALFSRGSGNI TGAIMKNEHA YFSAHPSEFG
     SQSDVSVGVS TLRTKLMHVL EQTMASSLAG TRDAISQELE EATYEFKVQY NDRPLSAESY
     LAESLDSFKH SFKAFAESFG RPQVREMLKN ELDQRVMDIL AQRYWNKPIE DLSAPLPELD
     PLSDLAKADP ESLYWHRKLD ASTSSLTKLG IGRLATTVVA NAIQSHVDRL IANSTFATHP
     YAQKQIVDAC NSILNDRFFS TSDQVENCIK PFKFEIEVED PEWAKGRENV SKVLKEELRA
     CETAFKRLED SIGRRKLKDV MSFIDKVRKG EVFLEGDGAG GAGGFSSALL ARGRESVFLR
     DRADLIKMRL LAVRSKQCSS KKNKYYCPEV FLDVVADKLT STAVLFLNVE LLSEFYYNFP
     RELDMRLGRH LSDAEVERFA REDPRIRNHL DVIRKKELLE LALQKIESIR QLDGRERKNR
     NSDRPVGNRE QRNRGWNLF
//