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Database: UniProt
Entry: F4WXB5_ACREC
LinkDB: F4WXB5_ACREC
Original site: F4WXB5_ACREC 
ID   F4WXB5_ACREC            Unreviewed;       627 AA.
AC   F4WXB5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE            EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN   ORFNames=G5I_10599 {ECO:0000313|EMBL:EGI61164.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI61164.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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; GL888423; EGI61164.1; -; Genomic_DNA.
DR   RefSeq; XP_011061513.1; XM_011063211.1.
DR   AlphaFoldDB; F4WXB5; -.
DR   STRING; 103372.F4WXB5; -.
DR   EnsemblMetazoa; XM_011063211.1; XP_011061513.1; LOC105150259.
DR   GeneID; 105150259; -.
DR   eggNOG; KOG1707; Eukaryota.
DR   InParanoid; F4WXB5; -.
DR   OrthoDB; 5481412at2759; -.
DR   Proteomes; UP000007755; 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; cd01893; Miro1; 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; 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; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51423; MIRO; 2.
DR   PROSITE; PS51419; RAB; 1.
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:UP000007755};
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        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..174
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
FT   DOMAIN          310..345
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          421..585
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
SQ   SEQUENCE   627 AA;  71149 MW;  069A44522227E260 CRC64;
     MVQRPVTSRR NVRILLIGER GVGKTSLILS LVSEEYAEEV PSKAEEITIP ADVTPEQVPT
     HIVDYSAVEQ TEDQLAEEIQ KAHVICVVYS VDDEDTLDRA ASYWLPLIRR CSPDNRCPVV
     LVGNKIDLVD YSTIEAVYPI MKEFTEIESC IECSAKTLQN VSETFYYAQK AVLHPTTPLY
     NYDTQELTEE CKTALQRIFK ICDVDNDGLL NDMELNAFQQ WCFNTPLQPQ VLEDVKAVLS
     KNICDGICNG CVTMKGFMYL QCLFIQRGRN ETTWAVLRKF GYDNELQMSK EYIHPSLKVP
     SGCSTELSHK GQEFLTLLFM QHDRDRDGAL SPLEMESLFS RCLFPPWGDE YKYTVATNEK
     GWITFQGYMC QWALLTLTNV RKTLEYMAYL GYNMYHNECQ TSSIVVTREK KVDLAKKQSS
     RNVYTCHVIG PKSSGKTTLC RTLVDPKLEK LNDKAVPSTA HVTVNTLHVY GQEKTIVLKD
     INVINVQDAL TPAEIQCDAA ALVYDASNPK SFEYIARIYI KYFADSKIPV LIVANKSDLS
     EVKQSYLLQP AAFCSKYKLM PPQPYSISRT IRREIFVKLA TMAAFPHINQ FGLMQGDSLV
     WWKAGLGIAI ATIAGYVMMR VLNTEKR
//
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