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Database: UniProt
Entry: A0A0J8QP23_COCIT
LinkDB: A0A0J8QP23_COCIT
Original site: A0A0J8QP23_COCIT 
ID   A0A0J8QP23_COCIT        Unreviewed;       626 AA.
AC   A0A0J8QP23;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-JUN-2023, entry version 29.
DE   RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE            EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN   ORFNames=CISG_04579 {ECO:0000313|EMBL:KMU74229.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU74229.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS268134; KMU74229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8QP23; -.
DR   STRING; 454286.A0A0J8QP23; -.
DR   Proteomes; UP000054559; 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:UP000054559};
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        597..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..174
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
FT   DOMAIN          415..581
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
SQ   SEQUENCE   626 AA;  69481 MW;  E2AAF939DDDE90FE CRC64;
     MGTGSSTVRI CVCGDEGTGK SSLITSLVKG VFVTNKIQPV LPQVTIPPTI GTPESVTTTT
     IVDTSALPQE RSNLAKELRK SNVILLVYSD HYSYERVALF WLPYFRSLGV NVPVVLCSNK
     SDLTTEGVDQ QTVEDEMLPI MTEFKEIDSC IRSSAREHRN VNEAFFLCQK AVTYPIAPLF
     DSKEAVLKPA AVNALQRIFY LCDKDHNGYL SDKEIDDFQI KCFGKPLNDD DLEHIKETIR
     RTYPQSVTPS GIDSQGFLHL NKLYVEKGRH ETVWIILRAF QYTDNLSLQE DFLHPRLEVP
     PFASAELSPA GYRFFVDLFL LCDKDNDGGL NDAELASLFA PTPGFPSSWT DDSFPSSTVR
     NEAGHVTLQG WLAQWSMTTF TSPKTTLEYL AYLGFESTDR SNPLNHGGTE DYQTTETATA
     SWTSAAGSGK SALLDAFLSR GFSPTYRPTI QPRTAVNTVE LPGGRQCYLL LDELGELEPA
     ILENRTKLLD QCDVIAYTYD SSDPDSFAYI PKLRAKYPHL EELPSVFIAL KADLDRTTQR
     AECQPDEYTS RLNMPGPPLH VSVRWNSIQE LFVHIAEAAM EPSTAFPRSE EDVEGKWMAW
     GIAIGAIVCA GAAAVVIWRR VAGSAS
//
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