ERAL1_CHICK
ID ERAL1_CHICK Reviewed; 461 AA.
AC Q8JIF5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GTPase Era, mitochondrial;
DE Short=GdERA;
DE AltName: Full=ERA-like protein 1;
DE Flags: Precursor;
GN Name=ERAL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA-BINDING.
RX PubMed=12618759; DOI=10.1038/sj.onc.1206287;
RA Gohda J., Nomura Y., Suzuki H., Arai H., Akiyama T., Inoue J.;
RT "Elimination of the vertebrate Escherichia coli Ras-like protein homologue
RT leads to cell cycle arrest at G1 phase and apoptosis.";
RL Oncogene 22:1340-1348(2003).
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; AB089163; BAC06859.1; -; mRNA.
DR RefSeq; NP_989570.2; NM_204239.2.
DR AlphaFoldDB; Q8JIF5; -.
DR SMR; Q8JIF5; -.
DR STRING; 9031.ENSGALP00000006355; -.
DR PaxDb; Q8JIF5; -.
DR GeneID; 374084; -.
DR KEGG; gga:374084; -.
DR CTD; 26284; -.
DR VEuPathDB; HostDB:geneid_374084; -.
DR eggNOG; KOG1423; Eukaryota.
DR InParanoid; Q8JIF5; -.
DR OrthoDB; 586738at2759; -.
DR PhylomeDB; Q8JIF5; -.
DR PRO; PR:Q8JIF5; -.
DR Proteomes; UP000000539; Unplaced.
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.
PE 1: Evidence at protein 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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..461
FT /note="GTPase Era, mitochondrial"
FT /id="PRO_0000404547"
FT DOMAIN 89..354
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 380..461
FT /note="KH type-2"
FT REGION 39..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..104
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 123..127
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 144..147
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 213..216
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 260..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..334
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT COMPBIAS 51..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 144..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 461 AA; 51135 MW; 1EA7145F2A6A294E CRC64;
MAAPWLQRWR GAYAGPSGPL RLVRLHGVQR SSWRAAHAAA GAFGAGPHPG PPQRAANPGP
GPHPPPVATS REKHARIVQG RPDQPAEPKV LRISIIGAPN SGKSTLSNQL LGRKVFPVSK
KVHTTRCKAR GVITHEDTQL IILDTPGLTS PMKAKRHKLE AAMLTDPWDS MKHADLVLVL
VDVSDHWTRN SLSLEVLKCL SQFPHIPSVL VLNKVDLLKK KIILLGLINE LTEGIVNGKK
LKVRSEFEYN SSSPAKTVLK VTQTPPPENR ARESPCQLET DKAQEGSSLD NSSDVKASES
SLDTEAREQK PYKYGDQKNR KGWPHFQDIF MLAALNGEEV DTLKQYLLMQ AKPGPWEFHS
RVLTSQSPHE ICDNIIREKI LEYLPLEVPY GVTQVTELWE EGPSGELIIV QNLVVPRKSH
KLMLIGRRGA LISRIAQEAG QDLMNIFLCD IRLKLKVEVK S
