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Database: UniProt
Entry: A0A0D2DR27_9EURO
LinkDB: A0A0D2DR27_9EURO
Original site: A0A0D2DR27_9EURO 
ID   A0A0D2DR27_9EURO        Unreviewed;       635 AA.
AC   A0A0D2DR27;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 38.
DE   RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE            EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN   ORFNames=Z517_06911 {ECO:0000313|EMBL:KIW80296.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW80296.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW80296.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW80296.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC       {ECO:0000256|PIRNR:PIRNR037488}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC       Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004200,
CC       ECO:0000256|PIRNR:PIRNR037488}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000256|ARBA:ARBA00007981, ECO:0000256|PIRNR:PIRNR037488}.
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DR   EMBL; KN846972; KIW80296.1; -; Genomic_DNA.
DR   RefSeq; XP_013284104.1; XM_013428650.1.
DR   AlphaFoldDB; A0A0D2DR27; -.
DR   STRING; 1442368.A0A0D2DR27; -.
DR   GeneID; 25306401; -.
DR   VEuPathDB; FungiDB:Z517_06911; -.
DR   HOGENOM; CLU_014255_3_0_1; -.
DR   OrthoDB; 5481412at2759; -.
DR   Proteomes; UP000053029; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd01892; Miro2; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR013566; EF_hand_assoc_1.
DR   InterPro; IPR013567; EF_hand_assoc_2.
DR   InterPro; IPR021181; Miro.
DR   InterPro; IPR020860; MIRO_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072:SF73; MITOCHONDRIAL RHO GTPASE; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR   Pfam; PF08355; EF_assoc_1; 1.
DR   Pfam; PF08356; EF_assoc_2; 1.
DR   Pfam; PF00071; Ras; 2.
DR   PIRSF; PIRSF037488; Mt_Rho_GTPase; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51423; MIRO; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR037488};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR037488};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037488};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037488};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|PIRNR:PIRNR037488};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW   ECO:0000256|PIRNR:PIRNR037488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR037488};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        606..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..169
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
FT   DOMAIN          421..589
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
SQ   SEQUENCE   635 AA;  70513 MW;  10E8014A4E463F4D CRC64;
     MATVRICVCG DEGCGKSSLI TSLVKDTFVS TRIQAVLPQI TIPPTLGTPE NVTTVIVDTS
     ALPQDRATLA KELRKSNVIL LVYSDHYSYE RVALFWLPYF RSLGVNLPVI LCANKSDLIT
     TSTSAQIVEE EMLPVMSEFK EIDSCIRTSA RDHFNVNEAF FLCQKAVTHP IAPLFDAKES
     VLKPAAVAAL LRIFYLCDKD KDGLLNDKEM EDFQVKCFDK GLSSEDLQHI KETIDNHIPG
     AASTRGITSQ GFLLLNKLYA EKGRHETIWV ILRTFQYTDS LSLEESFLHP KFEVPEYASA
     ELSPAGYRFL VDLFLTSDRD NDGGLRDEEL ASLFAPTPGI PQIWVDNNFP SCTMRNDAGH
     VTLQGWLAQW SMTTFTSPKT TLEYLAYLGF ESTDRSNTST TAALKLTKPR KRRRKPGRVG
     RNVLLAHVLG APQSGKSALL DAFLAQPFNN LYHPTIQPRV AVNTVELPGG RQCYLILKEL
     GESEAAVLEN KSKLLDQCDV IVYAYDSSDP DSFAYIPNIR KTYPHLEDLP SVYVALKADL
     DRTTQRSENQ PDEYVAQVQR MPQGPPISTS VTWPSIQELF VVISEAGLEP VTAYPRPLQE
     DDDGQLMRYG LALGVVVCAA AAAVVIWRRS AMPGS
//
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