ID A0A0F0IA11_ASPPU Unreviewed; 1251 AA.
AC A0A0F0IA11;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=P875_00011189 {ECO:0000313|EMBL:KJK64574.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64574.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK64574.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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}.
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:KJK64574.1}.
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DR EMBL; JZEE01000391; KJK64574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IA11; -.
DR STRING; 1403190.A0A0F0IA11; -.
DR Proteomes; UP000033540; 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};
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:UP000033540};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
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 1025..1066
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 398..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 138793 MW; F5F7EFBE669669BA CRC64;
MATVRICVCG DEGTGKSSLI TSLVKGVFVT NKIQPILPQI TIPPTIGTPE NVTTTTVVDT
SALPQERSNL AREIRKSNVI LLVYSDHYSY ERVALFWLPY FRSLGVNVPV VLCANKSDLA
ADHSEAQVIE EEMLPLMAEF KEIDSCIRTS AREHRNVNEA FFLCQKAVTH PIAPLFDSKE
SALKPAAVAA LQRIFYLSDK DRDGYLSDKE LEDFQMRCFE KPLSEEDLVH IKETIQKTHP
TSVAPSGIDC RGFIHLNKMY AEKGRHETVW IILRAFQYTD NLSLQESFLH PRFEVPPYAS
AELSPEGYRF FVNLFLLSDK DNDGGLNDAE LASLFAPTPG LPASWADGSF PSSTVRNEAG
HVTLQGWLAQ WSMTTFTSPK TTLEYLAYLG FESSDRSNPS TTAALKVTRP RKRRKRPGRV
GRNVVLGHVL GPPGSGKSAL LDAFLARGFS TTYHPTIQPR TAVNTVELPG GKQCYLILDE
LGELEPAILE NQVKLLDQCD VIVYTYDSSD PDSFAYIPEL RSKYPHLEEL PSVFVALKAD
LDRTTQRAEY QPHEYTAMLN MPSSPLHVSV TWSSMQEVFV HIAEAAMEPS TAFPRSEEDV
EGKWMAWGIA LGAVVCAGAA AVMIWRRCPT PTSASLYRTG CIRSWRVEWH GGSGRGDQQH
NQPSGGWLST AGRRRCVCDM AQGPSRASEL HYYRALDHAN AGFATGTYHL KDDLHLATPP
PHPSEAPVVN PNPLATVPTP PTSGVKLSLV SVGQRNKLPV FTSKEKVTAP PFADGNPALA
AIPTKDGLKR RKPKNNIIKS SSSFVSRVIT HEASSKRLND RNPDGLFAFA NINRAFQWLD
LSSKNKEEPL AKILFTKAHM LTHDINELTK SPSHIDIAMG SSAGDIIWYE PISQKYARIN
KNGVVSNSPV THIKWIPGSE NMFMAAHANG QLVVYDKEKE DALFTPEISN HSAEAMKASS
RLPLQVLKSV NSRNQKTNPV ALWKLANQKI SQFAFSPDQR HLAVVLEDGS LRVMDYLKEE
VLDIFRSYYG GLICVCWSPD GKYIVTGGQD DLVTIWSFPE RKIVARCQGH NSWVSTVAFD
PWRCDERTYR FGSVGDDCRL LLWDFSVGML HRPRAHQASA RQRTSMIASN TQHFNRHRAD
SASNRMRSDS QRTADTYNDY DSAVRHPVEP RARTALLPPI MSKIVGDDPI CWLGFQEDSI
MTSSLEGHIR TWDRPREGIN DSYNGNTSSP AISTSAAGSG SGIADSAMGS L
//
