ID B6GZR5_PENRW Unreviewed; 651 AA.
AC B6GZR5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN ORFNames=Pc12g09660 {ECO:0000313|EMBL:CAP80593.1}, PCH_Pc12g09660
GN {ECO:0000313|EMBL:CAP80593.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP80593.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP80593.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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,
CC ECO:0000256|PIRNR:PIRNR037488}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000256|ARBA:ARBA00007981, ECO:0000256|PIRNR:PIRNR037488}.
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DR EMBL; AM920427; CAP80593.1; -; Genomic_DNA.
DR RefSeq; XP_002557792.1; XM_002557746.1.
DR AlphaFoldDB; B6GZR5; -.
DR STRING; 500485.B6GZR5; -.
DR GeneID; 8304261; -.
DR KEGG; pcs:Pc12g09660; -.
DR VEuPathDB; FungiDB:PCH_Pc12g09660; -.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_3_0_1; -.
DR OMA; IILRKFH; -.
DR OrthoDB; 5481412at2759; -.
DR BioCyc; PCHR:PC12G09660-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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:0007005; P:mitochondrion organization; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; 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 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; IPR021181; Miro.
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; 2.
DR PIRSF; PIRSF037488; Mt_Rho_GTPase; 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 PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51423; MIRO; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR037488};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR037488};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037488};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037488};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR037488};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|PIRNR:PIRNR037488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037488};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
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}.
FT TRANSMEM 623..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..189
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 205..240
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 441..607
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
SQ SEQUENCE 651 AA; 72325 MW; 515859F3FC2D55D4 CRC64;
MASGMLSMCP TPRNTPNRPI RPVRICVCGD EGTGKSSLIT SLVKGVFVTN KIQPVLPQIT
IPPTLGTPEN VTTTTVVDTS ALPQERNNLA REIRKCNVIL LVYSDHYSYE RVALFWLPYF
RSLGVNVPVV LCANKSDLAT GHSETRVVEE EMLPLMAEFK EIDSCIRTSA REHRNVNEAF
FVCQKAVTHP IAPLFDSKEA ALKPAAVAAL QRIFYLCDKD RDGYLSDKEL KDFQIRCFSK
PLNEADLNHI KDTIQKAYPD SVTESGIDCQ GFIHLNKLYS EKGRHETVWI ILRAFQYTDN
LSLQEKFLHP KFEVPPYASA ELSPEGYRFF VNLFLLSDKD NDGGLNEAEL ASLFAPTPGL
PASWVDSSFP SSTVRNEAGH VTLQGWLAQW SMTTFLSPKT TLEYLAYLGF EPSDQSDQSI
TAALKVTRPR RKRRRPGRVG RNVVQCHVLG APGSGKSALL DALLSRGFST TYHPTIQPRT
AVNTVELPGG KQCYLILDEL GELEPALLEN QSKLLDQCDV IAYTYDSSDP DSFSYIPALL
AKYPHLEELP SVFIALKADL DRTTQRAEHQ PHEYTAMLNM PSPPLHVSVT WSSIQEVFVH
IAEAAMEPST AFPRSEEDVE GKWMSWGIAL GAVVCAGAAA VMIWRRVGSG N
//
