ID E9E0R5_METAQ Unreviewed; 627 AA.
AC E9E0R5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN ORFNames=MAC_03463 {ECO:0000313|EMBL:EFY90469.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY90469.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY90469.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC Probably involved in control of anterograde transport of mitochondria
CC and their subcellular distribution. {ECO:0000256|ARBA:ARBA00003481}.
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; GL698490; EFY90469.1; -; Genomic_DNA.
DR RefSeq; XP_007809803.1; XM_007811612.1.
DR AlphaFoldDB; E9E0R5; -.
DR STRING; 655827.E9E0R5; -.
DR GeneID; 19247774; -.
DR KEGG; maw:MAC_03463; -.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_3_0_1; -.
DR InParanoid; E9E0R5; -.
DR OMA; IILRKFH; -.
DR OrthoDB; 5481412at2759; -.
DR Proteomes; UP000002499; 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; IPR002048; EF_hand_dom.
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; SM00054; EFh; 2.
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; PS50222; EF_HAND_2; 2.
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:UP000002499};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..169
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 185..220
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 305..340
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 420..584
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
SQ SEQUENCE 627 AA; 70419 MW; 1EC1D298AC6D0CE3 CRC64;
MATVRICVCG DESTGKSSLI ASLVKDQFMS NKIQPVLPQI TIPPSIGTPE NVTTTIVDTS
ARPQDRTTLR KEIRKCNVIL LVYADHYSYE RVALFWMPYF RSLGVNVPVV LCANKSDLAG
QGNTPQIVEE EMLPVMAEFR EIDSCIRTSA REHKNVNEVF FLCQKAVTHP IAPLFDYKEG
RLKPACVAAL KRVFFLCDKD QDGFLNDQEM RDFQARCFDK PLTSDDLDNI KLSISKSMPD
ANMERGIDQS GFLQLNKIYA EKGRHETIWI ILRKYHYTDS LSLEDKFLHP RFDVPEYCSA
ELSPIGYRFF VDLFLLFDKD NDGGLNDQEL EALFSPTPGL PASWVDSSFP SSTVRNEGGH
ITLQGWLAQW SMTTFLEPKT TIEYLAYLGF ESPNVKDDIT AALKVTKSRK RRRRPGRVER
NVVLCYLIGA PGAGKSSLLD SFLNRPFEGL YHPTIKPRRA VNSVELPGGK QVYLIFEELG
ELEPAILENQ SKLDACDLIC YSYDSSDPDS FSHIVDVRSK YPHLDELPSV YTALKADKDK
TTQRSELQPD QYTSSLSMNT PLHVSVTWNS IAELFVALAE TATNPSMGFP KTEEEAPDRT
SLYLALGATA CAAVAAVMIW RRSTNAA
//
