ID F7W654_SORMK Unreviewed; 629 AA.
AC F7W654;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 28-JUN-2023, entry version 60.
DE RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN ORFNames=SMAC_06135 {ECO:0000313|EMBL:CCC12992.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12992.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12992.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12992.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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}.
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:CCC12992.1}.
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DR EMBL; CABT02000033; CCC12992.1; -; Genomic_DNA.
DR RefSeq; XP_003344851.1; XM_003344803.1.
DR AlphaFoldDB; F7W654; -.
DR STRING; 771870.F7W654; -.
DR GeneID; 10802169; -.
DR KEGG; smp:SMAC_06135; -.
DR VEuPathDB; FungiDB:SMAC_06135; -.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_3_0_1; -.
DR InParanoid; F7W654; -.
DR OMA; IILRKFH; -.
DR OrthoDB; 5481412at2759; -.
DR Proteomes; UP000001881; 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:0007005; P:mitochondrion organization; 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 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.
DR PROSITE; PS51419; RAB; 1.
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:UP000001881};
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 601..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..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 421..585
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
SQ SEQUENCE 629 AA; 70207 MW; A82CA2357A2ECB77 CRC64;
MSTAVRICVC GDEGTGKSSL IASLVKGVFV ANKIQAVLPQ VTIPPTTGTP ENVTTTIVDT
SARPQDRTTL RKEIRKSNVI LLVYSDHYSY ERVALFWMPY FRSLGVNVPV VLCANKADLV
SDGNAAQVAE EEMLPVMAEF REIDSCIRTS AKEQKNVIEV FYLCQKAVTH PIAPLFDYKE
GQLKPACVDA LRRIFFLSDK DQDGYLNDQE MQDFQQKSFD KPLSQEDLDN IKLTVSKAVP
SSSTDKGLDL QGFLQLNKLY AEKGRHETIW IILRKYHYTD SLSLEDNFLH PRFDVPDNAS
AELSPAGYRF FMDLFLTFDK DNDGGLNDRE LAALFAPTPG LPHSWAETSF PSTTVRNEAG
HITLQGWLAQ WSMTTFLEPK TTLEYLAYLG FETPNARETT TAALKITKPR KRRRRPGRVD
RNVVLCYILG SSGAGKSSLL DVFLNRPFDT LYHPTIKPRR AVNSVELQGG KQCYLILEEL
GELEPAILEN QAKLDACDLI CYAYDSSEPD SFSHIVELRK RYPQLDELPA VYTALKADRD
KTTQRSELQP DAYTAALNMS APLHVSVTWN SISELFVALA EAATNPSTAF PRSEDPPADR
ASLYMALGAT ACAALAVFMI WRRSTSNAA
//
