ID A0A168J1G7_CORDF Unreviewed; 1890 AA.
AC A0A168J1G7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=GTP-binding protein LepA {ECO:0000313|EMBL:OAA79915.1};
GN ORFNames=LEL_03401 {ECO:0000313|EMBL:OAA79915.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA79915.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA79915.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA79915.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- FUNCTION: Promotes mitochondrial protein synthesis. May act as a
CC fidelity factor of the translation reaction, by catalyzing a one-codon
CC backward translocation of tRNAs on improperly translocated ribosomes.
CC Binds to mitochondrial ribosomes in a GTP-dependent manner.
CC {ECO:0000256|HAMAP-Rule:MF_03137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03137}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03137}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03137}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. LepA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03137}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000256|ARBA:ARBA00005454}.
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:OAA79915.1}.
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DR EMBL; AZHF01000002; OAA79915.1; -; Genomic_DNA.
DR STRING; 1081108.A0A168J1G7; -.
DR OrthoDB; 5473535at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF7; TRANSLATION FACTOR GUF1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF06421; LepA_C; 1.
DR Pfam; PF04212; MIT; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03137};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03137};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03137};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03137};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|HAMAP-Rule:MF_03137};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03137}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 1291..1472
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 576..603
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 52..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1300..1307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1365..1369
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1419..1422
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ SEQUENCE 1890 AA; 206873 MW; 05678D663FE627C6 CRC64;
MPQHQPPHDH TGPPNSPPTA LVEFEEGNED TDTASAAVAA LRAFSATHLT LTRSKASVSP
PSSHLKTNSL LSAPRPPRTS SLLPPPRVLR KLPLEGDEST GSAETASAGH RYWHQQTADA
ATNKDPHELN TSPNQDGPWN THHPKHSQLH QRPAQTPHDR SESAVTQGLS QPLDESFRSG
ETEVGLHNHR VHQQSQPGGA PSVVPVKSLT SAVDRPRIGP LPPEQCSHQM PQDLPRDGQP
ARGHGRRRSS KGSTDADKAK AAKPPSQKAM LSRALQKANT AVQLDNAQNL EGARIAYSEA
CDLLQQVLRR TSGDEDKRKL EAIRQTYASR IEELDQIGPM QNHSTALKAL PARPGSDEYS
PELVQKQYNA ASIASNMISS GGKLAEGSST TRIYPRRPTS PASNTQQHDD DQPPPNIRAT
EWQRTAPNGQ QGMLQSSFSK PSSRSNHTPT GSQERALDMP PPLNSVSAAS PLKSPPGKNS
KYQQSHDFVR QSDSMDELGH ARDGSQNSWL DGIGESGGST ASSIHSRTSS EGLRRKHLRS
ASGQTEAEFD TALDAAIEAA YDDGYEPTGT DNIGEKDAGE EAVARVLRKV ERARERVRRR
EQETLSLSNG ADMAGLLSPR HYRSTHSRNG FYDDNSSDDE ERMLEEMARD YDIGDFTMSE
AVPIIVTRDE ECRSSTRHVE APPESRSQVE PVRSLMEKKS TSNVIKGLGP SLPPPNTSLP
ELPPPRGTSP MQSVRNRRLS GQNPKQLKID TTKPNPSPLV IHSHSDQLRA AREQENGRPS
TATGRIRTVS HARSTPSIDV TPSDPSSLLS MASHRIPTDL DEALPGKPAS PTATAHKLRK
NFSSSSLRSM KSRNMSLSNL EDPSDMSPGT PSSNQFGGSR TPAVPTIPTP MSSEFRDNLD
SSSTGARLFD DHFHQPTSPG SADNAHPDAP VPLEACPHDF MLRPFWLMRC IFQTLVHPRG
GYVSTKLFVP RDVWKVKGVK LKNIDDKIAN CDLLTAALLK LAQVDTCDAD AVLEEMQSLE
GILEQVQASL TRKLGNDVGV QGSGSLFKEA GGDGDGTSGV PRSGSVSNKP SFSWRRLRSK
SSGVALSGAY NSSRTAVGDA GKGDLGMASL PMTAQPTSRP PRRDLAQAQF IGPNANYMSS
LARLFDAAQA VDQIARQVDD PGLRHADKTQ VGLELCTRHA AEFFGFYICR FALADLVGPS
KHLDDQLRKE LWNSAVDLIA TTANDRDGNF YMNLVGRAAR AWTRQCLTSR PNATRRPDLD
RDCAAWVRRF ASQTKPSPAQ LEARMAAIPI ERYRNFCIVA HIDHGKSTLS DRLLEHTGTI
SASDANKQIL DKLDVERERG ITVKAQTCTM LYNYKGEDYL LHLVDTPGHV DFRAEVTRSY
GSCGGAILLV DASQGIQAQT VSNFHLAFAQ GLALLPVVNK IDMPSADVPS VLKQIQDSFE
LNPEEAVLVS AKTGKGIERV LPAVIEKMPH PLGDRSKPLK MLLVDSWYDN FRGVVLLVRI
FDGTIRAGDN VVSLGTGMKY TVGQVGVQYP DAIPQKVLSA GQVGYVHFNP GMKQIKDAKL
GDTFTVVGSE GSVDPCPGFD EPKPMVFVAA FPTDQGDYSR LADSINQLVL NDRSVTFQKD
HSEALGAGWR LGFLGSLHCS VFQDRLKQEH GRSIIITEPT VPTKIIWSNG KEEIVQNPAL
FPDTSHPHVK NSQLLEPFVK ATITVPEEHL GRVIELCEAN RGQQKSIEFF NKDQVILVYD
IPTAQLVEDL FGKLKGSSKG YATLDYEETG WRESKLSKVQ LLVNKQPVDA ICKIVHASQV
ERVGRQWVTK FKEHVDRQMF EVVIQAIAGN KIIARETIKP FRKDVLAKLH ASDISRRRKL
LEKQKDGRKR LRAVGNVIID QAAFQNFLAR
//
