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GEM1_ASPOR
ID   GEM1_ASPOR              Reviewed;         633 AA.
AC   Q2UM43;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Mitochondrial Rho GTPase 1;
DE            EC=3.6.5.-;
DE   AltName: Full=GTPase EF-hand protein of mitochondria 1;
GN   Name=gem1; ORFNames=AO090003000148;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC       Probably involved in control of anterograde transport of mitochondria
CC       and their subcellular distribution. {ECO:0000250|UniProtKB:P39722}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P39722}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:P39722}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR   EMBL; AP007155; BAE57372.1; -; Genomic_DNA.
DR   RefSeq; XP_001819374.1; XM_001819322.1.
DR   AlphaFoldDB; Q2UM43; -.
DR   SMR; Q2UM43; -.
DR   STRING; 510516.Q2UM43; -.
DR   EnsemblFungi; BAE57372; BAE57372; AO090003000148.
DR   GeneID; 5991357; -.
DR   KEGG; aor:AO090003000148; -.
DR   VEuPathDB; FungiDB:AO090003000148; -.
DR   HOGENOM; CLU_014255_3_0_1; -.
DR   OMA; HVSVTWN; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0032865; C:ERMES complex; IEA:EnsemblFungi.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0015886; P:heme transport; IEA:EnsemblFungi.
DR   GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:EnsemblFungi.
DR   GO; GO:0055091; P:phospholipid homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; IEA:EnsemblFungi.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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; PTHR24072; 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   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51423; MIRO; 2.
PE   3: Inferred from homology;
KW   Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..633
FT                   /note="Mitochondrial Rho GTPase 1"
FT                   /id="PRO_0000239331"
FT   TOPO_DOM        1..603
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        625..633
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..170
FT                   /note="Miro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   DOMAIN          186..221
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          306..341
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          422..588
FT                   /note="Miro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   REGION          398..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         115..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         321
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         431..438
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         467..471
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         537..540
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  70287 MW;  6DDD87E178C10521 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 AVMIWRRVSG SGT
 
 
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