ID A0A6G0V722_9BILA Unreviewed; 1555 AA. AC A0A6G0V722; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JUL-2024, entry version 16. 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=FO519_000555 {ECO:0000313|EMBL:KAE9556216.1}; OS Halicephalobus sp. NKZ332. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae; OC Halicephalobus. OX NCBI_TaxID=2598192 {ECO:0000313|EMBL:KAE9556216.1, ECO:0000313|Proteomes:UP000488831}; RN [1] {ECO:0000313|EMBL:KAE9556216.1, ECO:0000313|Proteomes:UP000488831} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NKZ332 {ECO:0000313|EMBL:KAE9556216.1}; RC TISSUE=Whole-body {ECO:0000313|EMBL:KAE9556216.1}; RX PubMed=31814372; RA Ragsdale E.J., Koutsovoulos G., Biddle J.F.; RT "A draft genome for a species of Halicephalobus (Panagrolaimidae)."; RL J. Nematol. 51:1-4(2019). CC -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211, CC ECO:0000256|RuleBase:RU361183}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}; 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}. 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:KAE9556216.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VOSG01000006; KAE9556216.1; -; Genomic_DNA. DR Proteomes; UP000488831; 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:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0097177; F:mitochondrial ribosome binding; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; 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; cd03709; lepA_C; 1. DR CDD; cd04280; ZnMc_astacin_like; 1. DR Gene3D; 1.10.10.1940; -; 2. DR Gene3D; 1.25.40.90; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 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; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR034035; Astacin-like_dom. DR InterPro; IPR006297; EF-4. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR038363; LepA_C_sf. DR InterPro; IPR013842; LepA_CTD. DR InterPro; IPR035654; LepA_IV. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR003582; ShKT_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; PF01400; Astacin; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF01417; ENTH; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF06421; LepA_C; 1. DR Pfam; PF01549; ShK; 2. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00273; ENTH; 1. DR SMART; SM00254; ShKT; 2. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51864; ASTACIN; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. DR PROSITE; PS51670; SHKT; 2. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_03137}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03137}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03137}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; 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|HAMAP-Rule:MF_03137}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03137}; KW Reference proteome {ECO:0000313|Proteomes:UP000488831}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}. FT DOMAIN 40..216 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT DOMAIN 663..801 FT /note="ENTH" FT /evidence="ECO:0000259|PROSITE:PS50942" FT DOMAIN 1227..1420 FT /note="Peptidase M12A" FT /evidence="ECO:0000259|PROSITE:PS51864" FT DOMAIN 1479..1515 FT /note="ShKT" FT /evidence="ECO:0000259|PROSITE:PS51670" FT DOMAIN 1519..1555 FT /note="ShKT" FT /evidence="ECO:0000259|PROSITE:PS51670" FT REGION 767..884 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 911..930 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 957..1003 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1029..1082 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1433..1479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 767..802 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 820..884 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 961..976 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1433..1450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1319 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 49..56 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137" FT BINDING 109..113 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137" FT BINDING 163..166 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03137" FT BINDING 1318 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 1322 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 1328 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" SQ SEQUENCE 1555 AA; 173697 MW; 2B406935A86053EB CRC64; MLEKWYFSCR YGFRFYCTNL KISRVNAGER LSSIESFTPD RIRNFGIVAH VDHGKSSLAD KLLQMTGVIT DQEQDQFLDK LQVERDRGIT VKAQTCSMVY KSHLLNLIDT PGHADFSFEV SRSLAVCDGV VFLVAANQGV QAQTLANFWL AFNNDLKMIP VINKIDIREA NVEAVQNQLN TLFDFQPEEV LRISAKNGVN IDTVLDTLIT RCPPPTVSPN DPFKALIFDS WYDQYRGAIA MISVKAGSIK KGQKISSFNE KKTYEVLEVL SAGQIGYIIC NMKTVREAAV GETLFDPVEQ DKVVPFPGFS AIQPTVYSGL FPVNSAQYED LRMAVERLCL NDPSVVITPD SSSALGLGWR VGFLGVLHME VFSQRLEQEY DADVILTSPS VEYRAIIKDN DTIRKKRYAG KGEIVFSDPS NFPELTDVEK FLEPVVQLTV IVPLEYLNTV NSLCSECRGE RGDVSFIDND RVIVKSKIPL AEVVVDFFER LKKLTSGYAS FDYEPTGYQE ANLVKLGVSI NGKHIDEFSL ITPSSQATAK AKTLVSKLKM EIPRQQYDVN IKATVGNSTK AIVQGTIRAY KKDFSQLLKG NFGGGGMERL NKKLSHQKKG KERMKMIGQI QVPKEAFINT MSDFLNGIAS LTKTVQDTLN SYEVRKISDK VQNYVMNFTE PEMKVREATS EEAWGPTPDM MREIAGLTFQ YDAFPEVMGM LWKRMLPPSP VAWRHTYKSL LLLEYLLKNG CERVIASARD HAFEMRSLER YKCTDERGRD QGVNEDDELL RQERLKAKSA SRDDKYRGYS RDDMVMRGGS NFSSSSKNYR SNRYDDEDCR NDGRYDRDDR FDDEKSNKRE VTSFGFDDEK RSASPELGIR LDSPHKDNDE DDEFGDFTVA RSNINNAAKT AGNNKDSFDF GGFASSLPPP PTSTTSKPAA SNKIIDDDLF GFSNAATAEK KKDEFDFLGL GSDSQPTSSI RPPSGPSSPT LGGDLFGAPS NSKPTDDFLF GAPSNSSKVS DDLFGISAPA KSVQDSSFDF LGLSSPSPGA QPFPSQTPQS KSDDFLNSLQ SVPPQTKSPD TKGTAGAQNN QANKSALWND LSGSLDLDNL LSTKPKQSMS MNEMKSRQGM TSCKEMRIRI FEFFVLLFFG LNNSLILANE LFDKSIPDEE THLTDMDFLA ARTFTDPGMF HGKVNDSAMY RKDRFEGDIV NSGLNGRTMK HFLEENGLGK IPGIMRNAVK QTYLMWTDGR IPYTISSQYS SFSRSKIAEA IEEYRRLTCI DFAPKSAADQ DYIHIVPDDG CYSLVGRIGG KQPVSLGDGC IQKGIIIHEL MHAVGFFHEQ SRADRDDYVT INWNNVEAGL QDQFDKYSLN MIDHLDTTYD YGSVMHYAST AFSKNGKPTI EPKKKGVEIG QRTGFSETDI YKINKLYKCS QFVSTTASPE DTLSEVLKPG NKTTDSSTDK GSGENPHEEI ENISGGVVSG GSGKGSGHCR DRRRDCEFLS RSGHCESRFS KKFMAENCPK SCHKCKSTCE DTRSWCERWA NSGMCTQSIF KEYMKQKCAK SCQLC //