ERAL1_BOVIN
ID ERAL1_BOVIN Reviewed; 437 AA.
AC A5PK43;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=GTPase Era, mitochondrial;
DE AltName: Full=ERA-like protein 1;
DE Flags: Precursor;
GN Name=ERAL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ovary;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:O75616}.
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; BC142348; AAI42349.1; -; mRNA.
DR RefSeq; NP_001092492.1; NM_001099022.2.
DR AlphaFoldDB; A5PK43; -.
DR SMR; A5PK43; -.
DR STRING; 9913.ENSBTAP00000020770; -.
DR PaxDb; A5PK43; -.
DR PRIDE; A5PK43; -.
DR Ensembl; ENSBTAT00000020770; ENSBTAP00000020770; ENSBTAG00000015639.
DR GeneID; 523344; -.
DR KEGG; bta:523344; -.
DR CTD; 26284; -.
DR VEuPathDB; HostDB:ENSBTAG00000015639; -.
DR VGNC; VGNC:28559; ERAL1.
DR eggNOG; KOG1423; Eukaryota.
DR GeneTree; ENSGT00390000013800; -.
DR HOGENOM; CLU_038009_2_1_1; -.
DR InParanoid; A5PK43; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 586738at2759; -.
DR TreeFam; TF321650; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000015639; Expressed in laryngeal cartilage and 105 other tissues.
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; IPR004044; KH_dom_type_2.
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; PF07650; KH_2; 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 2: Evidence at transcript level;
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_0000404545"
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 264..296
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; 48567 MW; 2F86DD6932F47C12 CRC64;
MAASSWRGAV LLRTVSGLWQ AGPDAAREWM TRLPSLLGFQ QRCVSCVAGP AFSGPRLASA
SRPNGQNSAL DCFLGLSQPD NSLPFRVPAV SVHRDEQDLL LVHRPDMPEN PRVLRVVLLG
APNAGKSTLS NQLLGRKVFP VSKKVHTTRS QALGVITEKE TQVILLDTPG LISPAKQKRH
HLELSLLEDP WKSMESADLV VVLVDVSDKW TRNQLSPQVL RCLTQFSQVP SILVMNKVDC
LKQKSVLLEL TAALTEGVVN GKKLKTKQAL RSRPDTHCPS PAAQGPNPQP VRDPQQMGWP
HFQEIFMLSA LSQEDVKTLK QYLLAQARPG PWEFHSEVLT SQTPEEICAN MIREKLLEYL
PEEVPYNVQQ KTVVWDEGPS GELVIEQKLL VSKESHMKIL IGPKGYLIAQ IAQEVGRDLM
NIFLCEVQLR LSVKLLK
