GEM1_CANAL
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 03-AUG-2022, entry version 109.
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 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; 538388at2759; -.
DR PRO; PR:Q5ABR2; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0032865; C:ERMES complex; IEA:EnsemblFungi.
DR GO; GO:0031307; C:integral component of 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:0015886; P:heme transport; IEA:EnsemblFungi.
DR GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:EnsemblFungi.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:EnsemblFungi.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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; PTHR24072; 2.
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 SMART; SM00054; EFh; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 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
