ID A0A091ETR1_CORBR Unreviewed; 408 AA.
AC A0A091ETR1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GTPase Era, mitochondrial {ECO:0000256|ARBA:ARBA00019149};
DE AltName: Full=ERA-like protein 1 {ECO:0000256|ARBA:ARBA00030975};
DE Flags: Fragment;
GN ORFNames=N302_03183 {ECO:0000313|EMBL:KFO59674.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO59674.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO59674.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO59674.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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. {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}.
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DR EMBL; KK718904; KFO59674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ETR1; -.
DR STRING; 85066.A0A091ETR1; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00367; GTPase_Era; 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 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, ECO:0000256|PROSITE-
KW ProRule:PRU01050};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU01050}; Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 40..302
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT REGION 48..55
FT /note="G1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 74..78
FT /note="G2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 95..98
FT /note="G3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 164..167
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 203..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..282
FT /note="G5"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT COMPBIAS 203..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO59674.1"
FT NON_TER 408
FT /evidence="ECO:0000313|EMBL:KFO59674.1"
SQ SEQUENCE 408 AA; 45325 MW; 5F32C3EAF9A0CA6D CRC64;
PAPGRPDPQR GLAASKPLLY LAEEQRRLLE NRPDQPQNPK VLRIAIIGAP NAGKSTLSNR
LLGRKVFPVS KKVHTTRCKA WGVITHEDTQ LIILDTPGLT NPLKAKRHNL DEAMLTDPWD
SMKHADLVLV LVDVSDHWTR NSLSREVLKC LSQFPHTPSV LVLNKVDILK KKFLLLEIVA
DLTEGIVNGK KLKVKSAFKQ DSSSSAKSPL QITQPSPPEG KVPQSPCGQE KNQAQEGSAL
DRSSVVGGAG TGEAQGPKYY GPEDLKDMKG WPHFQEIFML AALHGEEVDT LKRYLLMQAK
PGPWEFHSDV LTNQSPQEIC DNIIREKVLE YLPLEVPYGV TQVTDIWEEG ECGELLIVQS
LLVPRESHKR MLIGRGGKVI SRIAQEAGQD LMNAFLCDVR LKLKVEVK
//
