ID A0A2Y9JVK1_ENHLU Unreviewed; 354 AA.
AC A0A2Y9JVK1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GTPase Era, mitochondrial {ECO:0000256|ARBA:ARBA00019149};
DE AltName: Full=ERA-like protein 1 {ECO:0000256|ARBA:ARBA00030975};
GN Name=LOC111151350 {ECO:0000313|RefSeq:XP_022365018.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022365018.1};
RN [1] {ECO:0000313|RefSeq:XP_022365018.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022365018.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025227}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
CC Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000256|ARBA:ARBA00007921,
CC ECO:0000256|PROSITE-ProRule:PRU01050}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01050}.
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DR RefSeq; XP_022365018.1; XM_022509310.1.
DR AlphaFoldDB; A0A2Y9JVK1; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd04163; Era; 1.
DR CDD; cd22534; KH-II_Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTPase_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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42698; GTPASE ERA; 1.
DR PANTHER; PTHR42698:SF4; GTPASE ERA, MITOCHONDRIAL; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR PROSITE; PS51713; G_ERA; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 112..237
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
SQ SEQUENCE 354 AA; 39441 MW; 5771D7AB43B95946 CRC64;
MAAPSRRAAT LFWAVSGVRQ LGTNAARERG VRLSSLFDCQ RRCVSCFAGA AFSGPRLSSA
SRRYGQSSAL DRFLGLSQPD SSLTSHPPGV SMHRDEQDLL LVHHPNMPEN PRVLRVVILG
APNAGKSTLS NQLLGRKVFP VSKKVHTTRC QALGVITEKE AQVILLDTPG LISPVKQKRH
HLELSLLEDP WKSMESADLV VVLVDVSDKW TQNQLSPQLL QCLTQFSQIP SILVMNKQYL
LAQARPGPWE FHSGVLTSQT PEEICANIIR EKLLEHLPQE IPYSVQQRTV MWEEGPSGEL
VIEQKLLVLK ESHVRILIGP KGRLISQIAQ EVGRDLMDIF LCDVQLRLSV KLLR
//
