ERAL1_AILME
ID ERAL1_AILME Reviewed; 437 AA.
AC D2GU20;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=GTPase Era, mitochondrial;
DE AltName: Full=ERA-like protein 1;
DE Flags: Precursor;
GN Name=ERAL1; ORFNames=PANDA_000103;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Probable GTPase that plays a role in the mitochondrial
CC ribosomal small subunit assembly. Specifically binds the 12S
CC mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating
CC the 3' terminal stem-loop region. May act as a chaperone that protects
CC the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small
CC subunit assembly (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Mitochondrion
CC inner membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=Localizes on the matrix side on the mitochondrial
CC inner membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
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DR EMBL; GL192339; EFB26121.1; -; Genomic_DNA.
DR RefSeq; XP_002912360.1; XM_002912314.3.
DR AlphaFoldDB; D2GU20; -.
DR SMR; D2GU20; -.
DR STRING; 9646.ENSAMEP00000004861; -.
DR Ensembl; ENSAMET00000005057; ENSAMEP00000004861; ENSAMEG00000004602.
DR GeneID; 100463961; -.
DR KEGG; aml:100463961; -.
DR CTD; 26284; -.
DR eggNOG; KOG1423; Eukaryota.
DR GeneTree; ENSGT00390000013800; -.
DR HOGENOM; CLU_038009_2_1_1; -.
DR InParanoid; D2GU20; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 586738at2759; -.
DR TreeFam; TF321650; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISS:UniProtKB.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
PE 3: Inferred from homology;
KW GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..437
FT /note="GTPase Era, mitochondrial"
FT /id="PRO_0000404544"
FT DOMAIN 112..330
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 360..437
FT /note="KH type-2"
FT REGION 120..127
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 146..150
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 167..170
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 236..239
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 271..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..310
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 120..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 167..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75616"
SQ SEQUENCE 437 AA; 48260 MW; E4F57F378377D61A CRC64;
MAAASGRAVT LLRVVFGVRQ LGPTAAREWG ARLSSLFDCQ RRCVSCFAGA SFSGPRLASA
SRHHGQSSAM DCFLGLSQPD GSLTSRPPGV SMHRDEQDLL LVHRPDMPEN PRVLRVVLLG
APNAGKSTLS NQLLGRKVFP VSKKVHTTRC QALGVITEKE AQVILLDTPG LISPVKQKRH
HLELSLLEDP WKSMESADLV VVLVDVSDKW TRNQLSPQVL QCLTQFSQVP SILVMNKVDC
LKQKSVLLEL TAALTEGVVN GKKLKMRQAL RSQPGTPCPS PAVKGPNTQS VGGPQRIGWP
HFQEIFMLSA LSQEDVKTLK QYLLAQARPG PWEFHSGVLT SQTPEEICAN IIREKLLEHL
PQEMPYSVQQ RTVMWEEGPS GELVIEQKLL VPKKSHVRIL IGPKGHLISQ IAQEVSRDLM
DIFLCDVRLR LSVKLLQ
