ID A0A0A2KYI9_PENEN Unreviewed; 1187 AA.
AC A0A0A2KYI9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=PEX2_014720 {ECO:0000313|EMBL:KGO61976.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61976.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61976.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61976.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO61976.1}.
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DR EMBL; JQFZ01000027; KGO61976.1; -; Genomic_DNA.
DR RefSeq; XP_016602642.1; XM_016738748.1.
DR AlphaFoldDB; A0A0A2KYI9; -.
DR STRING; 27334.A0A0A2KYI9; -.
DR GeneID; 27674167; -.
DR HOGENOM; CLU_005336_0_0_1; -.
DR OrthoDB; 5481412at2759; -.
DR PhylomeDB; A0A0A2KYI9; -.
DR Proteomes; UP000030143; 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:UP000030143};
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 990..1031
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1081..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 131788 MW; 5058C7B634A124A2 CRC64;
MASVRICVCG DEGTGKSSLI TSLVKGVFVT NRIQPVLPQI TIPPTLGTPE NVTTTTVVDT
SALPQERNNL AREIRKCNVI LLVYSDHYSY ERVALFWLPY FRSLGVNVPV VLCANKSDLA
TGHSETRVVE EEMLPLMAEF KEIDSCIRTS AREHRNVNEA FFVCQKAVTH PIAPLFDSKE
ASLKPAAVAA LQRIFYLCDK DRDGYLSDTE LKDFQIRCFS KPLNEADLNH IKETIQKAYP
DSITESGIDC KGFIHLNKLY SEKGRHETVW IILRAFQYTD NLSLQEKFLH PKFEVPPFAS
AELSPEGYRF FVNLFLLSDK DNDGGLNEAE LASLFAPTPG LPASWADGSF PSSTVRNEAG
HVTLQGWLAQ WSMTTFLSPK TTLEYLAYLG FEPSDQSDQS ITAALKVTRP RRKRRRPGRV
GRNVVQCHVL GAPGSGKSAL LDALLSRGFS TTYHPTIQPR TAVNTVELPG GKQCYLILDE
LGELEPALLE NQSKLLDQCD VIAYTYDSSD PDSFSYIPAL LAKYPHLEEL PSVFVALKAD
LDRTTQRAEH QPHEYTAMLN MPSPPLHVSV TWSSIQEVFV HIAEAAMEPS TAFPRSEEDV
EGKWMSWGIA LGAVIITSLA YTTTSVLPPP PPRYTIPVAY AAGAANGMAV PVVETNNTIT
HPERGCPLQV GEGTYILQDD LLLATPPPHP SEAPIINPNP LATLPTPPTT GVKLSLVTLD
LRKKPPTFLR SGVTAPQFGD GNPALAAPPV AAKDASKRRK PKNNIIKSSS SFVSRVITHE
TSAKRLGDRD SNGIFAFANI NRAFQWLDLS SPTKEEHLTK VLFTKAHMLC HDINEITKTS
SHLDIVMGSS AGDIIWYEPM SQKYARINKN GVINNSPVTH IKWLPGSENL FIASHANGVL
VVYDKEKEDA LFTPEANGHS EQEFGRLPLD ILKSVNSKNQ KTNPVSFWKM ANQKISSFSF
SPDQRHLAVV LEDGSLRLMD YLKEEILDIF RSYYGGLICV CWSPDGKYIV TGGQDDLLTI
WSFPERKVVA RCQGHNSWVS SVAFDPWRCD QKTYRFGSVG DDCRLLLWDF SVGMLHRPRA
HHASTRNRSS IVVPNSQTAN RHRADSGDNR VRSDSNQTES FNEDIDHTAS HPVEPRSRTA
LLPPIMSKIV GEDPICWLGF QKDCIMTSSL EGHIRTWDRP SDSVVKS
//
