ID A0A1J8QJZ1_9AGAM Unreviewed; 1111 AA.
AC A0A1J8QJZ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AZE42_03442 {ECO:0000313|EMBL:OJA12092.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA12092.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA12092.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA12092.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OJA12092.1}.
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DR EMBL; LVVM01004818; OJA12092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QJZ1; -.
DR STRING; 180088.A0A1J8QJZ1; -.
DR OrthoDB; 5481412at2759; -.
DR Proteomes; UP000183567; 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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd01893; Miro1; 1.
DR CDD; cd01892; Miro2; 1.
DR CDD; cd00198; vWFA; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
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; IPR020860; MIRO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24072:SF73; MITOCHONDRIAL RHO GTPASE; 1.
DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF08355; EF_assoc_1; 1.
DR Pfam; PF08356; EF_assoc_2; 1.
DR Pfam; PF00071; Ras; 2.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00054; EFh; 2.
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 SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51423; MIRO; 2.
DR PROSITE; PS50234; VWFA; 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 Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 2..178
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 168..203
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 288..323
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 397..560
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 668..868
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 960..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 122996 MW; BF8D73145F2486E3 CRC64;
MRRDVRILLV GDEGVGKSTI VTSLIKESFV AHVQHVVPEV TIPPEVTPEN VTTYIVDSGA
GPQDRQHLES EVRKAHVICV VYSIDNPHSF DRIPTYWLPL FRQLGVNVPV ILVGNKIDLR
GGEEVETCVE CSAKLPLNVS EVIYFAQKAV LHPTAPLYDS REHVLKPACV SALKRIFKLC
DANKDGVLDA AELNEFQRKC FDVPLQLQEL EGIKDMVREH AEGGVRDNGL TEDGFLYLHT
IFIQRGRLET TWTVLRKFGY AEDLRLTEAF LLPKFDVPHD CSVELSPQGY QFFTDIFETF
DKDQDGALNN AELEELFSTS PGNPWASQNF PDTTLVDGKG AVTLQGWLAQ WSMTTLLNHK
TTLSYLAYLG YPDEQRTSAL LTTRPRKVDR RKGKVTRNVF LCYVCGAAGS GKTSLLRSFA
GKPFRETYEP TSKMVSVVNA VDIDGSEKYL VLQEFGSKYE AETLRASKKT DFADVIVYVH
DSSDTNSFSY ISNLRQQYNL DHIPTLLVAT KSDLDLAQQR HEVQPDVYCR RLGLQVPVAV
SVKTEQVADV FHAICSIAMN PHAAIPGGAD RAMTASERLR VYVTFTALLG GASAGLVMLY
RSLLRPGGAI LPSWTTPWAT WLLDVISQLN SCKMEHIMDE DMDFDANAAQ KTPQFHDESY
YDGRKMLDLV FVQDCTGSQG SYISSATKNI QDICAHIFES GKLQSQEDLR VGLVAFRDHP
PQDHTYVVKN FGFSSDISKV HKDLAGLYAS GGGDGPEAVT AALAEVLHME WREHASKMVV
LIADAPPHGI GEYGDGFDEG SPDGHDPLQV VREMASRGIT LYATDFYQAI TTITSGLMLP
LTTADLLSHA IVGSVLENLD MERLVREVGH AVAQRILGNN ESVDDVAREL HEKLLLRNES
TKKVVIESIY KESPEAVHNV AVFTHASSLR EARPQLQRVH GSRFTEKYLL ARQTANRNLY
TYPYSPPTPA RSTTEKRYST MVPSSPPSAP SSPPRKVVQD FAAFGAPKNA SVFGTAVAST
PFSLAGGKAA FGGMRTSSSR SMFDVDDEDE EDDGRQKVEL KEDSISLDQV GPIRDLACHL
IVLIAVSHTT HSTGQTHRHA KRLAERARMI I
//
