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Database: UniProt
Entry: W7I726_9PEZI
LinkDB: W7I726_9PEZI
Original site: W7I726_9PEZI 
ID   W7I726_9PEZI            Unreviewed;       338 AA.
AC   W7I726;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Mitochondrial GTPase 1 {ECO:0000256|PIRNR:PIRNR006230};
GN   ORFNames=DRE_02682 {ECO:0000313|EMBL:EWC48103.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC48103.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC48103.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC48103.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial GTPase involved in assembly of the large
CC       ribosomal subunit. Plays a role in expression of the mitochondrial
CC       translational machinery. {ECO:0000256|PIRNR:PIRNR006230}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|PIRNR:PIRNR006230}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR006230}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR006230}.
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DR   EMBL; KI966406; EWC48103.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7I726; -.
DR   HOGENOM; CLU_011106_0_1_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   CDD; cd01856; YlqF; 1.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR016478; GTPase_MTG1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45782; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 1; 1.
DR   PANTHER; PTHR45782:SF4; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 1; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006230; MG442; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|PIRNR:PIRNR006230, ECO:0000256|PIRSR:PIRSR006230-
KW   1}; Mitochondrion {ECO:0000256|PIRNR:PIRNR006230};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006230,
KW   ECO:0000256|PIRSR:PIRSR006230-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT   DOMAIN          135..199
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
FT   REGION          310..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
FT   BINDING         194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006230-1"
SQ   SEQUENCE   338 AA;  37712 MW;  3A57BAD01A4AEA4F CRC64;
     MASTASFVPR TVFPRLDSII KSYYLGHHKA GLTKMRQLLS SVELIIECRD YRVPLSSRNP
     MFEKHLIGRE RMIVYTKRDL GAESLDQKTR ENIRRWHAPQ KVLFTDCKTD NDIKKVINYA
     KDIARAVDSL TGTRMMLTGM PNVGKSSLLN ALRRVGMHKG KVAITGGQPG VTRNIGTTVR
     ISSDPSILLY DTPGVFIPYV PNESTMLKLA LVGCVKDTLI DPVTLCDYLL FRINMVNPSL
     YAAYHPPTNN ITELLTATAL QTGRLGKGGV PDITATAIWL IQRYRIGELG RFILDDVDAD
     ALERRIEEES KEGMSANQLR KGVKAERAAH RASKANID
//
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