ID   A0A1X2I595_9FUNG        Unreviewed;       862 AA.
AC   A0A1X2I595;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN   ORFNames=BCR42DRAFT_423581 {ECO:0000313|EMBL:ORZ09526.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ09526.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ09526.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ09526.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ09526.1}.
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DR   EMBL; MCGE01000027; ORZ09526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2I595; -.
DR   STRING; 90262.A0A1X2I595; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000193560; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        736..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          259..532
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   COILED          801..828
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   862 AA;  96822 MW;  D4D8EA7379B0149F CRC64;
     MSDIYGVPSS MLGARRHLRR NSAPYIDGIC DDSNDSSAPP LKPLDLSRSK MFSPASSILN
     SPIAMSPSSS TSSIRSAART HQYRMNAAQE HRTYHDSCQR LLTHIASVTS ICDELYRNNK
     DRAVYYPPFP KAQHNQRMPP QRSMTTSALL ASSSDLMSLE TTSQPDMDCT SSLTDSLCNR
     RSSIQSDNLA SSTSTLVGMD SVHTGFLKQE FNILHLDLKV GHESTNLHTA LEKSSIANLL
     DEKLQQCKRH LDNLFNRVAD TSSKVLVTGD LNAGKSTFVN ALLKRELLPA DQQPCTNMFC
     EVLDANINDG LEQVHAIPHV EKYDRLDPST YHLVEMRHLD SLIMDFEDRY QILKIYTNDA
     RASQESLLHN GIIDIAMIDS PGLNTDSVKT TAVFARQEEI DVVVFVVSAE NHFTLSGKEF
     LWNAANEKAH IFIVVNRFDS IRDKDRCKRM ILEQIRQLSP ATYEDADDLV HFVSAGNVDL
     EPGSRKLDAP DFARLEERLR AFVLGNRTKS KLLPAKNYLV KFLLDIGVLS EANQADAANN
     HKLASERLEL DMPVYEQLLR GRDQLLHQVE RLAEGTVATI QQQTVERLQG AADQVQRAID
     TLEYPGIFLI WQYAQDLCES MAQVMLQDIR AAEQQARQDT QQCLDNLHEE AETQLGAFPC
     VANVDGMFLR PRDHHLVVQV ETTDFFDFAL DDKFSGCVLS MGAAAMVGGR VMGFKDTVSS
     LWNMSSMMGA QNMRRLALPM VGLAGASFLI YVVADMRNAV ERKLVRKFKE AVRDAGYVDA
     QSHRLGRGAR KVLRVEGWEI QSRLQKAIET KEQQRNELKT VLQTSQEAMD YFASLLEKST
     MLLDKVEAIH IDQTKIEEPL KM
//