ID   GEM1_CANAL              Reviewed;         716 AA.
AC   Q5ABR2; A0A1D8PCC5; Q5ABF5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 3.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Mitochondrial Rho GTPase 1;
DE            EC=3.6.5.-;
DE   AltName: Full=GTPase EF-hand protein of mitochondria 1;
GN   Name=GEM1; OrderedLocusNames=CAALFM_C100890WA;
GN   ORFNames=CaO19.13437, CaO19.6016;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC       Probably involved in control of anterograde transport of mitochondria
CC       and their subcellular distribution. {ECO:0000250|UniProtKB:P39722}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P39722}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:P39722}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR   EMBL; CP017623; AOW25786.1; -; Genomic_DNA.
DR   RefSeq; XP_718978.1; XM_713885.2.
DR   AlphaFoldDB; Q5ABR2; -.
DR   SMR; Q5ABR2; -.
DR   STRING; 237561.Q5ABR2; -.
DR   EnsemblFungi; C1_00890W_A-T; C1_00890W_A-T-p1; C1_00890W_A.
DR   GeneID; 3639354; -.
DR   KEGG; cal:CAALFM_C100890WA; -.
DR   CGD; CAL0000185710; GEM1.
DR   VEuPathDB; FungiDB:C1_00890W_A; -.
DR   eggNOG; KOG1707; Eukaryota.
DR   HOGENOM; CLU_014255_3_0_1; -.
DR   InParanoid; Q5ABR2; -.
DR   OrthoDB; 5481412at2759; -.
DR   PRO; PR:Q5ABR2; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0032865; C:ERMES complex; IEA:EnsemblFungi.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0015886; P:heme transport; IEA:EnsemblFungi.
DR   GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:CGD.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:EnsemblFungi.
DR   GO; GO:0055091; P:phospholipid homeostasis; IEA:EnsemblFungi.
DR   GO; GO:1900428; P:regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:CGD.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; IEA:EnsemblFungi.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; PF13202; EF-hand_5; 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; 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; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..716
FT                   /note="Mitochondrial Rho GTPase 1"
FT                   /id="PRO_0000239332"
FT   TOPO_DOM        1..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..713
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        714..716
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3..224
FT                   /note="Miro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   DOMAIN          240..275
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          388..423
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          505..671
FT                   /note="Miro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   REGION          58..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         84..91
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         113..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         167..170
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         257
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         259
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         264
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         401
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         403
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         405
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         412
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         514..521
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         550..554
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         620..623
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   716 AA;  81157 MW;  63AFA5AC93C4E19E CRC64;
     MSPDAIRVVV CGDDAVGKSS LITSLIKETI IEPQTNNVLP PITISRNDYI ESSQEYLNDQ
     DHHHHHQSSP STMKNKRKHN NKRERERERE SSINNVQPNE ISEYIPNITT IIDTSSSDMT
     NLQKELKRAD VIWLVYSDHY TYERISLHWM PLFRSMGVNL PIILCANKSD LFPKSKSNLK
     STNSDEFVPL INEFKEIEAG VRCSAKNNYN VVEAFYLCQR AVTHPISPIF DAKEGNLKPG
     AIKPLKRIFW LSDTDQDGYL NFEELSELHK KCFGIEASKS DYEEIVNLID QKILPSYNTT
     IETQTPPQQQ HLATSAGTPN GTTTTTSKGI SEDGFILLNK IYAESGRHET VWCILRAYHY
     TNSLSLSDKF LYPRLDVNPH SSVELSPTGY KFFVDLFIKF DKDNDGGLNE DELNTLFRST
     PGIPKLWVES NFPSSIVCNE EGYVTLQGWL AQWNLTTFLS YKTTLEYLAY LGFDEGNSTK
     ALKVTKPRKI RQKNGKTYRN AVNDRNVFNC FIVGAPKAGK SSLLESFLHG SYSDIYSPTI
     QPRLVVKDIE LRGGKQCYLI LEELGELEPA ILENKSRLDQ CDVICYAYDS SDPESFQYLV
     ELREKHGHLL DEVPAVFVAL KADLDKQQQR CDVQPENYTR DLFLNSPLHV SLAWNSSLHE
     MFIQLVDAAK TPSSATPGIE LEVSVDQDDI KHIIMTGAAI AVVGLVSIWV LNSLRR
//