ERAL1_SALSA
ID ERAL1_SALSA Reviewed; 457 AA.
AC B5X2B8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=GTPase Era, mitochondrial;
DE AltName: Full=ERA-like protein 1;
DE Flags: Precursor;
GN Name=eral1;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(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; BT045187; ACI33449.1; -; mRNA.
DR EMBL; BT059676; ACN11389.1; -; mRNA.
DR RefSeq; NP_001133545.1; NM_001140073.1.
DR AlphaFoldDB; B5X2B8; -.
DR SMR; B5X2B8; -.
DR STRING; 8030.ENSSSAP00000071032; -.
DR GeneID; 100195044; -.
DR KEGG; sasa:100195044; -.
DR CTD; 26284; -.
DR OrthoDB; 586738at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR Bgee; ENSSSAG00000063416; Expressed in zone of skin and 14 other tissues.
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 SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..457
FT /note="GTPase Era, mitochondrial"
FT /id="PRO_0000404549"
FT DOMAIN 107..350
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 376..457
FT /note="KH type-2"
FT REGION 115..122
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 141..145
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 162..165
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 231..234
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 270..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..330
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT COMPBIAS 270..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 162..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 231..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 50510 MW; 8FBFB32F3B9C7CC7 CRC64;
MAFRVSISTF GKSLRVRRVA NVSAPLANAS PFLRTGWAAR PPGTNNGHGF RFTPACFITS
DAFLSRLAKG KAETDDTHYH HPASVLPDSA EQLSLLVKDP DQPENSKVLR VAIIGAPNAG
KSTLSNQLLG RKVFAVSKKV HTTRARALGV LTEDDTQIIL LDTPGLTTPT KVKRHQLEKS
LLEDPWNTVK EAGLVVVMVD VSDKWACNKL DFEVLKCLTQ HPDVPAVLVL NKVDLLKSKS
RLLEITADLT CGVVNGRKLQ VRRVIKPPWA ERRTDREART SGSGDEEKPG GDVADGEGSE
ALSGLSKEQL RALKTQQGWA HFKDVFMVSA VDGEDVETLK RYLVVGAKPG SWQYHSDVLT
DQTPEEICTN TVREKLLEYL PKEVPYTMTQ AIDLWHDREN GELDIAVKLY VKKESHMKMV
IGQAGQMVAR IAREAGDDLS TVFLREVKLR LSVKVKN
