ID   A0A0F0ILC4_ASPPU        Unreviewed;       932 AA.
AC   A0A0F0ILC4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Dynamin family protein {ECO:0000313|EMBL:KJK68609.1};
GN   ORFNames=P875_00075860 {ECO:0000313|EMBL:KJK68609.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK68609.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK68609.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001270};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004374}.
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:KJK68609.1}.
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DR   EMBL; JZEE01000033; KJK68609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0ILC4; -.
DR   STRING; 1403190.A0A0F0ILC4; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:UniProt.
DR   CDD; cd00882; Ras_like_GTPase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027094; Mitofusin_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR   PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          283..572
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  102522 MW;  35DF4FDCC457FE0A CRC64;
     MSQEYFPGNG GSSAGEGSSR HPPQQEAPEY PFFPNAPPAY MTVGNGSTSE SATALMASLN
     RDSGYGDSIA SGSVRDGDAG GDWRTDMMVD RPTPMHTPTL PGQWNPAAEH ERQVVASHVH
     QLLYNSNRTK LGRAITRTLE TLKDLQDMNR QWPAHYPSVR DARDYPSDRP ALRQAQSFFD
     DGDIQQGDFK PGPIRRAATV SNSGDLAAAE SSAAAERRPA PEPRLMTPQI AQEFSILKLD
     LKLGALSQVE LVHSLEKASI ASLLDGKISQ SVKHLLSLRD RIEDTSSKVL ITGDLNAGKS
     TFCNALLRRK VLPEDQQPCT SIFCEVLDAR ENSGVEEVHA VHKDVDYNRN DESTYDVYPL
     TELENIVIDN SKYMQCKVYV KDVRTIDESL LNNGVVDIAL IDAPGLNSDS LKTTAVFARQ
     EEIDVVVFVV SAANHFTLSA KDFIHNAAKE KAYMFIVVNG FDQIRDKQRC ERMILDQINK
     LSPRTYKESA ELVHFVSSNA VPVAPPMSVE SSGSGGGGGF DSDGDDDDDD SKPKGKGKDK
     GKEKQKIQDF ENLESSLRRF VLEKRSRSKL APARTYLLNL LGDLNSLASV NRDIAQSELK
     RVTEELAELE PAYEGGQKKK IELDVQVEKN IDDSCEDVYN HTRSTLSDTI ARVSEADLGV
     EYPGIFSAFQ YAEDLKLAML EQISAAASAC EDYARVKTVD GVEAIQKIGL LHVGDKFAPL
     NFRADMMFRR SRRHTFAKQV DTEVELLDFF DIAGIWERQE KVAGTGMAMT AVTVLGGRLF
     GGISWVDSAF SAAKFLGPNN LRRLLVPGIV AAAALTAAYV LSTIPTTLPP RLSRKIAAAL
     EEKDYVHSNA TRISTEVRRV LRIPANNLQA SLAQDIEDLG RRKQEVSKTK VESENASKYF
     SNLFRESGEN RRSVESIDLD GPLPGAMGAH EP
//