ID A0A024RAJ7_HUMAN Unreviewed; 732 AA. AC A0A024RAJ7; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 02-DEC-2020, entry version 58. DE RecName: Full=Ribosome-releasing factor 2, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03059}; DE Short=RRF2mt {ECO:0000256|HAMAP-Rule:MF_03059}; DE AltName: Full=Elongation factor G 2, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03059}; DE Short=EF-G2mt {ECO:0000256|HAMAP-Rule:MF_03059}; DE Short=mEF-G 2 {ECO:0000256|HAMAP-Rule:MF_03059}; GN Name=GFM2 {ECO:0000256|HAMAP-Rule:MF_03059, GN ECO:0000313|EMBL:EAW95747.1}; GN Synonyms=EFG2 {ECO:0000256|HAMAP-Rule:MF_03059}; GN ORFNames=hCG_38200 {ECO:0000313|EMBL:EAW95747.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:EAW95747.1}; RN [1] {ECO:0000313|EMBL:EAW95747.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAW95747.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of CC ribosomes from messenger RNA at the termination of mitochondrial CC protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis CC follows the ribosome disassembly and probably occurs on the ribosome CC large subunit. Not involved in the GTP-dependent ribosomal CC translocation step during translation elongation. {ECO:0000256|HAMAP- CC Rule:MF_03059}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03059}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP- CC Rule:MF_03059}. 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; CH471084; EAW95745.1; -; Genomic_DNA. DR EMBL; CH471084; EAW95747.1; -; Genomic_DNA. DR RefSeq; NP_733792.1; NM_170691.2. DR SMR; A0A024RAJ7; -. DR Antibodypedia; 44237; 134 antibodies. DR GeneID; 84340; -. DR CTD; 84340; -. DR EuPathDB; HostDB:ENSG00000164347.17; -. DR HOGENOM; CLU_002794_4_1_1; -. DR BioGRID-ORCS; 84340; 87 hits in 844 CRISPR screens. DR ChiTaRS; GFM2; human. DR GenomeRNAi; 84340; -. DR Bgee; ENSG00000164347; Expressed in quadriceps femoris and 219 other tissues. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule. DR GO; GO:0032790; P:ribosome disassembly; IEA:UniProtKB-UniRule. DR CDD; cd16262; EFG_III; 1. DR CDD; cd03713; EFG_mtEFG_C; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_03059; mEF_G_2; 1. DR InterPro; IPR030851; EFG2. DR InterPro; IPR041095; EFG_II. DR InterPro; IPR009022; EFG_III. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR035649; EFG_V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_III; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00231; small_GTP; 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 Elongation factor {ECO:0000313|EMBL:EAW95747.1}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_03059}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03059}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03059}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_03059}. FT DOMAIN 68..353 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT NP_BIND 77..84 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059" FT NP_BIND 141..145 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059" FT NP_BIND 195..198 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059" FT COILED 270..290 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 411..431 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 732 AA; 81200 MW; 15869E090CB0848A CRC64; MLTNLRIFAM SHQTIPSVYI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVM KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL ERISRLLLPF ADQHVEIPSL TAGNIALTVG LKHTATGDTI VSSKSSALAA ARRAEREGEK KHRQNNEAER LLLAGVEIPE PVFFCTIEPP SLSKQPDLEH ALKCLQREDP SLKVRLDPDS GQTVLCGMGE LHIEIIHDRI KREYGLETYL GPLQVAYRET ILNSVRATDT LDRTLGDKRH LVTVEVEARP IETSSVMPVI EFEYAESINE GLLKVSQEAI ENGIHSACLQ GPLLGSPIQD VAITLHSLTI HPGTSTTMIS ACVSRCVQKA LKKADKQVLE PLMNLEVTVA RDYLSPVLAD LAQRRGNIQE IQTRQDNKVV IGFVPLAEIM GYSTVLRTLT SGSATFALEL STYQAMNPQD QNTLLNRRSG LT //