ID A0A2J5HX24_9EURO Unreviewed; 1267 AA.
AC A0A2J5HX24;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BDW42DRAFT_185105 {ECO:0000313|EMBL:PLN81979.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN81979.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the regulatory network controlling carbon source
CC utilization through ubiquitination and deubiquitination involving creA,
CC creB, creC, creD and acrB. Required to prevent the proteolysis of the
CC CreB deubiquitinating enzyme in the absence of carbon catabolite
CC repression. CreB deubiquitinating enzyme stabilized in a complex with
CC the CreC leads to the expression of genes such as those in the proline
CC and quinate pathways. {ECO:0000256|ARBA:ARBA00037241}.
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 -!- SUBUNIT: Interacts with creB. {ECO:0000256|ARBA:ARBA00038682}.
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 WD repeat creC family.
CC {ECO:0000256|ARBA:ARBA00038107}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000256|ARBA:ARBA00007981}.
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DR EMBL; KZ559531; PLN81979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HX24; -.
DR OrthoDB; 5481412at2759; -.
DR Proteomes; UP000235023; 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 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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR001806; Small_GTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR14107:SF16; AT02583P; 1.
DR PANTHER; PTHR14107; WD REPEAT PROTEIN; 1.
DR Pfam; PF08355; EF_assoc_1; 1.
DR Pfam; PF08356; EF_assoc_2; 1.
DR Pfam; PF00071; Ras; 2.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51423; MIRO; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 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, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT TRANSMEM 604..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..170
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 186..221
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 422..588
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT REPEAT 1042..1083
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 400..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 140079 MW; 9B3F03F91D017E9B CRC64;
MTPVRICVCG DEGTGKSSLI TSLVKGVFVT HKIQPILPQI TIPPTIGTPE NVTTTTVVDT
SALPQERSNL GREIRKANVI LLVYSDHYSY ERVALFWLPY FRSLGVNVPV VLCANKSDLA
VGHSEAQVIE EEMLPLMAEF KEIDSCIRTS AREHRNVNEA FFLCQKAVTH PIAPLFDTKE
STLKPAAIAA LQRIFYLNDK DRDGYLSDKE IKDFQMRCFE KALSEEDLIH IKDTILKTHP
TSVTPSGIDC PGFIQLNRLY AEKGRHETVW IILRAYQYTD NLSLQESFLH PRFEVPPYAS
AELSPEGYRF FVNLFLLSDK DNDGGLNDAE LASLFAPTPG LPASWADGSF PSSTVRNEAG
HVTLQGWLAQ WSMTTFQSPK ETLEYLAYLG FESADRSNQS TTAALKVTRP RKRRRRPGRV
GRNVVLGHAL GAPGSGKSAL LDAFLSRGFS TTYHPTIQPR TAVNTVELPG GKQCYLILDE
LGELEPAILE NQAKLLDQCD VIVYTYDSSD PDSFAYIPAL RSKYPHLEEL PSVFIALKAD
LDRTTQRAEY QPHEYTAMLN MSSPPLHVSA TWSSIQEVFV HIAEAAMEPS TAFPRSEEDD
EGKWMSWGIA LGAVVCAGAA AVMIWRRTRC LYQRKPAWSS TVCGATLGGI ITAAPLRRYA
PDLSCPYAVI FIIPLRSQNV LPPPPPRYTI PIAYAAGASN GMPVPVVETN NVIRHPEGGC
PLQVGEGTYH LKDDLHLATP PPHPSEAPIV NPNPLQTLPT PPTSGVKLSL VSFGQRAKTP
VHKPKENGHT PLFGEGNPVL ASTPVKEGVK RRKPKNNIVK SSSSFVSRVI THEAVSKRLN
DRNPDGIFAF ANINRAFQWL DVSSKNKEEP LAKILFTKAH ILSHDVNDLT KGPSHIDVVM
GSSAGDIIWY EPISQKYARI NKNGVVNGTS VTHIRWIPGS ENLFVAAHAN GQLVVYDKEK
EDALFVPEIH HPSAETGQLP LQVLKSVNSR NQKTNPVAVW NLAKQKITQF AFSPDHRHVA
IVLEDGSLRV MDYLKEEVTD IFRSYYGGLI CVCWSPDGKY IVTGGQDDLV TIWSLPERKI
VARCQGHNSW VSTVAFDPWR CDERTYRFGS VGDDCRLLLW DFSVGMLHRP RAHQASARQR
NSLIAPLPHT NRHRADSAGN RIRSDSQRTA DADGDYDHAV RHPVEPRART ALLPPIMSKI
VGEDPICWLG FQEDSIMTSS LEGHIRTWDR PREGLNDSYN AHASSSAISA SVAGSGSGRG
GSTMGSL
//
