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Database: UniProt
Entry: M5BQR3_THACB
LinkDB: M5BQR3_THACB
Original site: M5BQR3_THACB 
ID   M5BQR3_THACB            Unreviewed;      1492 AA.
AC   M5BQR3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Mitochondrial Rho GTPase 1 {ECO:0000256|ARBA:ARBA00019119};
DE   AltName: Full=GTPase EF-hand protein of mitochondria 1 {ECO:0000256|ARBA:ARBA00032646};
GN   ORFNames=BN14_02808 {ECO:0000313|EMBL:CCO28810.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO28810.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO28810.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(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: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}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004200}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000256|ARBA:ARBA00007981}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCO28810.1}.
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DR   EMBL; CAOJ01003813; CCO28810.1; -; Genomic_DNA.
DR   HOGENOM; CLU_249093_0_0_1; -.
DR   Proteomes; UP000012065; 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:0016043; P:cellular component organization; IEA:UniProt.
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; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR013566; EF_hand_assoc_1.
DR   InterPro; IPR013567; EF_hand_assoc_2.
DR   InterPro; IPR002048; EF_hand_dom.
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; 1.
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; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51423; MIRO; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          877..1045
FT                   /note="Miro"
FT                   /evidence="ECO:0000259|PROSITE:PS51423"
FT   DOMAIN          1196..1231
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          43..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1492 AA;  163662 MW;  9DD20DA04B503670 CRC64;
     MASTQVDLLS MTSIIQDRSG NSSSEHVDLG SFAPDANALR EAALKSRRKK KAVATEQLAS
     IPNQQIAEAD ASQPPVRPPV DEDSSMHDAT IPVVDMPNPQ EALTETEDGE IPESKPGSET
     NGIRPSEGDP REKTPRPPSS LSPRSTSIPD IAEVPGNIRQ GLDMTFRDLE EAKRLILDLL
     GLGVTPEYLV DCGVSPQCLA VCFYELNLRF PLNLDRRQIN LPPLYDLDKH MKDSQRREQI
     IRKRDRGRAP PRTIPPAIST IMEQTRSSHH AKALSPTPPD MEDKPLDELS PPSRLDTTPV
     AGIQLPDNTQ SLPSKDLDTS LMEDQKRMEL LARKAAMESI NKKRAAKAST LSSNNSDQPG
     TPYPMEISDV ESAVDALLAS VRMNSEPSNH SEGNFDKEYE GGSASTGEQL SDYDSDAMVE
     DELETRSPSP SDPEVDELMD DTAFSDSQRN VSPDPIPPTP LPVSSPKLTL ARVRFDALDH
     TRSSSLPAQP TPIAVPVVAR RSRPIASDFI DQAPPRPASA STAGTERSAL LKRKRSFVDP
     AVWPKRIVID LDSSDDEDDQ DEAGSSGSKN NTDRTPSRAA SNDQTATNGQ DQAAQMLLEK
     ELQIKAMMQK IKMRELQKKK PTSGSRTPLT GTVTPAVTTD TSKVVPSTTE LTSSPITSTM
     NLTPTETPSS QAPPIIPVAA QGEYKHYVHF RLLFTFEKVE MPSLVQKGKD SVLDSSLDTV
     SPKLDKGKGK ALEPEGVSQG AFSYATPALW LTSVSDNVTI SFTDESENNP RHGQLANSNS
     EQAPVRTTYR YAVLVYSYFI LSDADVLELS RPWLQTHFKA YVSPLAGFTS PNLQPSSPTD
     HQLSTIFWMS SSAGQDLNRQ LCTYEFPSGV CKNEICKDIH VRDFRASDGV GKSTIVTSLI
     KEEYVDNVQH VVPEVTIPPE VTPENVTTYI VDSSAAPADR PHLESEIRKA HVICVVYAID
     NPNSFDRVPT YWLPYFRSLG VNVPVILVGN KIDLRGGEVS NEDLENEVAP IMEEFKEVET
     CVECSARIPT NIAGIIFFAQ KAVLHPTAPL YDSREHTLKP AAVDALRRIF RLCDTNKDGA
     LIPFEQTCFK ASLQPQEVEG IKSILRSHDP SMLRPIPSPA HASPNGSPPP TPSVEEGVTE
     DGFLYLHTEF IRRARVETTW IVLRQFGYAE DLRLTESWLS PKFEVPHDCS VELSPQGYQF
     FTDIFQIFDR DQDGALRPEE LENLFNTSPG NPWAAEDDEG VDGTITLQHW LAKWSMTTLL
     DHKKTLAYLA YLGYNTGPTT GALKITKPRR AERRKDKVTR NVFLCYIVGA AGSGKTSLLN
     AFRQLAGGGI ETSISKDAPK SKGKGIGELG PYNPTEKVLS VVGAVELRGA EKYLVMQEFG
     SKSEANMLRD PKIMNLADVI IYVHDSSDTN SFSYISGLRR HEVQPDVYCR RLGLQGPYSV
     SVKNPQNLFL EIVATAINPL SAIPGGAERA SATLARRKIA LSVMGVVGGQ TG
//
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