ID A0A0D2ALZ4_9EURO Unreviewed; 635 AA.
AC A0A0D2ALZ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JUN-2023, entry version 37.
DE RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN ORFNames=PV06_06580 {ECO:0000313|EMBL:KIW40981.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW40981.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW40981.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW40981.1,
RC ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
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; KN847337; KIW40981.1; -; Genomic_DNA.
DR RefSeq; XP_016261197.1; XM_016407717.1.
DR AlphaFoldDB; A0A0D2ALZ4; -.
DR STRING; 215243.A0A0D2ALZ4; -.
DR GeneID; 27358654; -.
DR VEuPathDB; FungiDB:PV06_06580; -.
DR HOGENOM; CLU_014255_3_0_1; -.
DR OrthoDB; 5481412at2759; -.
DR Proteomes; UP000053342; 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:UP000053342};
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; 70857 MW; D458686CA15A5879 CRC64;
MATVRICVCG DEGCGKSSLI TSLVKDTFIS NRIQAVLPPI TIPPTLGTPE NVTTTIVDTS
ALPQDRTNLA RELRKSNVIL LVYSDHYSYE RVALFWLPYF RSLGVNLPVI LCANKSDLVT
SSTPAQIMEE EMLPVMSEFK EIDSCIRTSA REHYNVNEAF FLCQKAVTHP IAPLFDAKES
VLKPAAVAAL LRIFYLCDKD KDGLLNDKEM QDFQLKCFDK SLSAEDLQHI KDTIEHHLPG
AALGRGITSQ GFLMLNKLYA EKGRHETIWV ILRIFQYTDS LSLQESFVHP KFEVPEYASA
ELSPAGYRFL VDLFLTSDRD NDGGLKDEEL GALFAPTPGI PQLWIDNNFP SCTVRNDAGH
VTLQGWLAQW SMTTFMSPKT TLEYLAYLGF ESPDRSNSST IAALKLTKPR KRRRRPGRVG
RNVLLAHVLG APQSGKSALL DAFLARPFNE LYHPTIQPRV AVNTVELPGG RQCYLILKEF
GESEAAALDN KSKLLDQCDV IVYTYDSSDP DSFAYIPNIR KNYPYLEDLP SVYVALKADL
DRTMQRVDHQ PEEYTAQIQR MPQGPPISTS VTWPSIQDLF VVLSEAGLDP VTAYTRLLEE
DDGGQLMRYG LVLGVVVCAG AAAVVIWRRS TSPTM
//
