ID A0A498LXM1_LABRO Unreviewed; 275 AA.
AC A0A498LXM1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Elongation factor mitochondrial {ECO:0000313|EMBL:RXN13278.1};
GN ORFNames=ROHU_028674 {ECO:0000313|EMBL:RXN14395.1}, ROHU_029037
GN {ECO:0000313|EMBL:RXN13278.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN13278.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN13278.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN13278.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN13278.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN13278.1}.
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DR EMBL; QBIY01012990; RXN13278.1; -; Genomic_DNA.
DR EMBL; QBIY01012909; RXN14395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498LXM1; -.
DR STRING; 84645.A0A498LXM1; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR047872; EFG_IV.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 1: Evidence at protein level;
KW Elongation factor {ECO:0000313|EMBL:RXN13278.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000313|EMBL:RXN13278.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498LXM1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 46..166
FT /note="Translation elongation factor EFG/EF2"
FT /evidence="ECO:0000259|SMART:SM00889"
FT DOMAIN 168..255
FT /note="Elongation factor EFG"
FT /evidence="ECO:0000259|SMART:SM00838"
SQ SEQUENCE 275 AA; 30433 MW; C7CE05212B556245 CRC64;
MKKVMKKCSV EQTKDEEKLP VTVTATVTEM RGFDFLFCAI APPPLKETPQ LDYTAETLFD
FTHKKQSGGS GQYGKVIGVL EPLDPENYTK LEFSDETVGT NIPKQFVPAV ERGFREACEK
GPLTGHKISG VRFILEDGAH HMVDSNEISF IRAGEGALKQ AIEKSSVVIL EPVMSVEIVA
PNEFQGAVIA GVNRRHGVIT GQDGAEGYFT LYADIPLNDM FGYSTELRSC TEGKGEYTME
YSRYQPCLPS VQEELVNKHL EATGQLPAKK SKWKN
//