ID   V5EVK8_KALBG            Unreviewed;       949 AA.
AC   V5EVK8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN   ORFNames=PSEUBRA_SCAF20g03073 {ECO:0000313|EMBL:EST07303.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST07303.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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}.
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DR   EMBL; KI545863; EST07303.1; -; Genomic_DNA.
DR   RefSeq; XP_016292292.1; XM_016436252.1.
DR   AlphaFoldDB; V5EVK8; -.
DR   STRING; 1365824.V5EVK8; -.
DR   GeneID; 27418889; -.
DR   eggNOG; KOG0448; Eukaryota.
DR   HOGENOM; CLU_011752_0_0_1; -.
DR   OMA; RCERMIL; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000019377; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000019377}.
FT   DOMAIN          251..522
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          27..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          229..256
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  103695 MW;  D35EB64890CA0C62 CRC64;
     MTDNNTSQQY ATPVKKVLRS QTWNDSASHN LTVASPSTPA SNSTATDGGQ LFQSKPRHID
     QARAQQDAQQ AFAQHTSEFE ESRDKLLGTI DTTSTLLADL RDFNKNKRLI HYAAADDAHK
     ASSSSQSHKR SHSNSQHSLE EADANLHTSS VDSAHRPMPP AFMRLNTTGG HASLPSTPAR
     NALTNQQSQN DDESDESTDM SVLKLDLRVG SVAVNPQALM RSLERSSVAQ LLDGRMEKSE
     RHLENLKQRL SDTQSKVLVT GDLNAGKSTF VNALLRRPLM PTDQQPCTTV FCEVLDASEL
     NGNVEEVHML KQGVKYSSQD DSTFTRHTLE EVEQIVAEAE EVSPEDAPIL KCYAHDTRAT
     QDSLLKNGIV DIALIDAPGL NRDSLKTTAL FARQEEIDVV VFVVSAENHF TLSAKEFLWN
     ASHDKAFVFI VVNKFESIKN KDKCRKLVLD QIRQLSPRTY EDAASLVHFV DSQAVFGAES
     DSSAAPDTPS EELGRKVEGG STIESRSSES LQSFARLEAA LRDFVLLKRA KSKLLPSKTY
     MLRLLSDIIF LAKINTQVAQ IELAEATKAL EVARPELAKC QASQQKLETV VEGEEDEAVT
     AVMQEAQRKL SSAIDLIGNG KPAIEAVQLP VYPGLFNVGQ YAQEVRHALT SSLELALRSV
     EDTARGTASQ AVDRVQKLGL VHLPDNDAEK RQRIFNPDVM FAKRRAMPGL VGLGLGSQVV
     QVQPSDFFDA YHHFTIVTGG SLSQDQSDKK DKSSHDELSL VSSLSLGLGA LTLVGGKTLG
     VKSAVDTLVR ISDLVGNPTA RRWAGPVFAV VSTGLVVYFI YDLPNSVPRN IGRSIKSGLQ
     SGTLLRSNDS AALTTLAPSA SSSSAQGEEA SFTAVHSARV GRETRKVLRL ASWDLQERFR
     VAIAQRRAEV EKQEAKQASA NLAIDWFDKT TSRVIQIRGQ VDEVKGLEA
//