ID A0A2P6THV6_CHLSO Unreviewed; 2921 AA.
AC A0A2P6THV6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Translation factor GUF1 homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03137};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_03137};
DE AltName: Full=Elongation factor 4 homolog {ECO:0000256|HAMAP-Rule:MF_03137};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_03137};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000256|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000256|HAMAP-Rule:MF_03137};
GN ORFNames=C2E21_7237 {ECO:0000313|EMBL:PRW33873.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW33873.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW33873.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:PRW33873.1}.
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DR EMBL; LHPG02000015; PRW33873.1; -; Genomic_DNA.
DR STRING; 3076.A0A2P6THV6; -.
DR OrthoDB; 5473535at2759; -.
DR Proteomes; UP000239899; 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 CDD; cd07473; Peptidases_S8_Subtilisin_like; 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; 3.40.50.200; Peptidase S8/S53 domain; 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
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; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 2.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS51892; SUBTILASE; 2.
DR PROSITE; PS00138; SUBTILASE_SER; 2.
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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 1328..1512
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 2433..2452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2475..2533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2549..2586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2638..2677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2781..2808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2825..2864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2588..2615
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2435..2452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2483..2532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2638..2653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2794..2808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2828..2860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT BINDING 1337..1344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1401..1405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
FT BINDING 1455..1458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137"
SQ SEQUENCE 2921 AA; 314307 MW; 6741189D0359200C CRC64;
MLLQAEFRKG RGPLLHVETI LGRLMASGRE WVLRCGVRGL LVELNPRFSY LQGAALLREL
ERSYLAILDV RAAEVSVLAA RSLAEPAYQQ RLQQVAAESD SSGVEAKLKQ LKANPAVEHA
QPEYIYYHTA QRFPNDTRFA EGDHSSGQWY LRQIDTGVRR SHQDLSANIV DGWNRAVIDE
NGQQRQPLLG TALYRDFSDT MGHGSHTAGT VGAVGNNGVG VAGMNWKVSL FVCKAASPSG
SLYESAVLDC LYLCRKEGVH VLSNSYAGGG FSEFQYEAIA KLRDAGALFV AAAGNEYTSN
DDVASFPASY QLDNVVSVAA ADADDTLAIF SNWGKSSVHL AAPGTMVLNT WNGNDADYEY
ASGTSMATPL VAGAAALLWS AKPTATFAQV KAALMQGVDK QPALLNRVIS GGRLNVARSL
AKLLRQANPL PPPQPATSWV VERNVGYNGS FFQGVMFSTA TPEECLQLCQ ILPWCAVVTA
FLQNETMAGR AQTESITGNC RMHDQAFAFT GVGLYPAALS AYRRGGTPVI AKPARLTAPL
GSWASPIDIT TTNFTSKAYT TYVQDYSPVP CVNERNRVRV FRWFSGSLPA GYANASSCPY
TVGDPVLSVL SSPNRTGGPY TCVGGQDDDA DVKCQNGHEF SYTFEFQPNT YYFLAVAPYG
ISGDSALTWF KLSLQVFPGS DPPVRQPYAG KGSWQNPIAV GNGPAGLPYL SPVLKDNSWS
VKTPQPIECS PFAQDTAVIF RWFSGNVSSG TVLTATSCEH SYFDPAVVVL KSVSLNATPT
TLSCVGSNDN SLVPCTGTTD TATAFTATLV VQPNTYYWFA VVPSLDLTTV RLRLRLSCQP
PATGTWANPV VISAMPFASQ KLCAYHQAVP PVKCAEGRNM SMVFRWFSGD QAGMATASSC
GNTTGDAVVS VLFSTRPTGG FTCISGNDDD FACPSNSATV GAFGMSFQFR PYTYYWLAVA
PRSEFNPSQV QLKVSIEVDS GVRRTHEDLK ANIVDGWNRA VYGDNTDSPW QPEQGSDLYT
NYTDHNARAH VVLFSNGGGS YSQVMFDSIA KMRDAGALVV APAGNSYVST DDVPFYPASY
KLDNVISVAS SNADDTLTTY SNWGLKTTHL AAPGSLILST TYNSDSSYGV TSGTSMSAPV
VTGAAALIWS ARPGATYQQV KKYKYYAALD VDQGFNPGVQ PVKCAEGRNS SVVFSDNLEC
PFNKGSVGAF GYKFPFKPFT YYWFAVGPKS ELAASQPVFA RFELDMITCN AAWAALQQLL
PPAQPAYSVF RGWQPGAFSL LQRLGCASSA AQPEGQGTAA APATLDSAVD PSKGFARGGY
SVGRFSPDRI RNFSIIAHVD HGKSTLADRL LEATGAIAAG GQAQYLDKLQ VERERGITVK
AQTVSLVYRY RGADYLLNLI DTPGHVDFSY EVSRSLSACQ GALLLVDASQ GVQAQTVANF
YLAWEQDLAI VPVLNKIDMD SADPQRVAQQ LKDAFDIEPQ DCLHVSAKTG LGLQSVLPAV
VERIPAPWGE PEGDLKMLLF DAYHDEYRGV VCLVEVKDGR VQTGDRITAA STGTNYEVIE
VGLLAPDPYP TGELLTGQVG YMLVGMKDTR QARVGDTWHH YRRPVEPLPG FKPAKSMVFA
GIFPLSAAGF EQLQAAMERL TLNDASVTVR RENSNALGAG FRCGFLGLLH MDVFRQRLEQ
EHGASVIVTA PTVPCRIMLP GGETVELQNP AEFPTNTKIA AVWEPTVAAT IVTPNDYVGS
IMTLCQDRRG DMLEHAVLGT GRTLLKYHLP LAELGGDFYD ELKSISSGYA SFDYEEAEYR
QADLQRMDIL INGEAVDALA RVVHREKAQN VGRRLVAKLK DLMDRQQFEV VLQAQAGGRI
VARETMKAFR KNVLAKCYGG DVSRKRKLLE KQKEGKKRMR RLGSVDVPQE ADQRQGLLVC
RSWAAVLSSC RAWRALALQM PIDAVVPPSP ALIAWLRRVR VRRLEFVQRP SERGDALCAQ
GFASSEQRYR ASIATLLATL EFISHSAGCL RELAGVHPRE GILVLTPFKA LERICMTGNA
SETCKLEVLS ELPRLHEVVA AGYGEYTTEG LPPSVRHLSL QWAVNSATSF QTIAFVVPEG
CQLASLALCS QRPLCLAAPS LARCARLTAS ARRVYLGLPL RNGAPWADVD EIAARWAQFM
LGGTLEAVEI TATRFFVFQP VQDVFDLATN EGLGGVVQHE QLATVLLARH FQSLHVEQRA
LAVGAFREFM RITRRCAEPV AFSFSAPLHR EQLDFLRQHA LATSISFGPV SRCDAITVLN
CPAFAARNGP LLQQLSHLEL SSQLDLAPYT ALQSMQGTWQ SEPQAPLGAT QLSSLRITPP
LGAAVVQRSF QSRWLRGVQR LGSLTLLRFA CADLSHLRGT ASAISLSSLQ PPSGVVSADS
LVLPPGGFGA DCTLALRMAY APPHAIHGLQ AAPGQPVQHQ MQQQQQPGGQ QLGQAAAVAA
QAAAWAQMAF HAAAPQAALQ APPPPQQVAQ QQQQQQQQQQ QQQQQQQQQQ QAHAAAPPAQ
QQAQQPQQAQ QEVVEMLEED AVIDLVDSDD EVEQVQQPPQ QPPPQQAQQA QQAQQPAAPA
GAAALAAAQQ VQQHAQQVQQ HAEQVQAAAE QHAQQAVQVL DNLGMAMQAV DLAMPPLEAE
SSDDDDELQG LMDASDDEAG FLPPLAPQLG GGPPAGAPGG GLGPWILVQP QVPLHLQGLP
QGLLQHLAAG QAGGPQLGGP LGGPLGGAAM WELQPWEMPD DRLSDVTIRH DALFGAAGTL
SVHAGALTVV YTGSGPEDLM ALLTHGPSRS SAGGPGRGSP SSSGSSGVLR TLRLSARSMR
FVAVRGSSAE GNEQQQSAAV AGGPASPAGQ QQQQQVAGAP QDHEVHSCSG VELFDYLSNT
DWSSQWDIKL QRSMFRDQLT FSLARRATPA DTPGLPVPAT V
//
