ID IF2_PARUW Reviewed; 920 AA. AC Q6MD64; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 22-JUL-2008, entry version 34. DE RecName: Full=Translation initiation factor IF-2; GN Name=infB; OrderedLocusNames=pc0761; OS Protochlamydia amoebophila (strain UWE25). OC Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae; OC Candidatus Protochlamydia. OX NCBI_TaxID=264201; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15073324; DOI=10.1126/science.1096330; RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., RA Rattei T., Mewes H.-W., Wagner M.; RT "Illuminating the evolutionary history of chlamydiae."; RL Science 304:728-730(2004). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Protects formylmethionyl-tRNA from spontaneous CC hydrolysis and promotes its binding to the 30S ribosomal subunits. CC Also involved in the hydrolysis of GTP during the formation of the CC 70S ribosomal complex (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the IF-2 family. 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; BX908798; CAF23485.1; -; Genomic_DNA. DR RefSeq; YP_007760.1; -. DR GeneID; 2781082; -. DR GenomeReviews; BX908798_GR; pc0761. DR KEGG; pcu:pc0761; -. DR NMPDR; fig|264201.1.peg.761; -. DR HOGENOM; Q6MD64; -. DR BioCyc; CPRO264201:PC0761-MON; -. DR GO; GO:0003924; F:GTPase activity; IEA:HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:HAMAP. DR GO; GO:0006413; P:translational initiation; IEA:HAMAP. DR HAMAP; MF_00100; -; 1. DR InterPro; IPR015760; aIF-2. DR InterPro; IPR000178; IF2. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR000795; ProtSyn_GTP_bd. DR InterPro; IPR005225; Small_GTP_bd. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR PANTHER; PTHR23115:SF41; aIF-2; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 2. DR Pfam; PF04760; IF2_N; 1. DR TIGRFAMs; TIGR00487; IF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01176; IF2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Initiation factor; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 920 Translation initiation factor IF-2. FT /FTId=PRO_0000228221. FT NP_BIND 427 434 GTP (By similarity). FT NP_BIND 473 477 GTP (By similarity). FT NP_BIND 527 530 GTP (By similarity). FT REGION 421 569 G-domain. SQ SEQUENCE 920 AA; 101783 MW; 67B581DDB0A94631 CRC64; MAKNLKLNIK NAQIAEAINL SGLKSKLAKK KEEESTQKSS AAKSTSKTTK TEVEELPKEE APRIRARSKS AFAEAPADQS SKEITEEIKT SQDEESISRE AAKVIEEKSR MKTSAEIRQE IFGEELSQAP SKDSSQELEF AEKIKTNETK PTTFIEPTIA SPAPAEPKSL VEDKTSITHV YQNQKRDIPI RESLPPQEKL GPTGKHMRDF IKPKPQPERV SRPLEANNSN QKEVSEANKE KLDKNKIKPK SKGFEEPKVL TADDDARKGL KSPKFKEFKD IKPARKPETR QFDARDRQGL RTSDEDQHWR KKKNKQRQNI QEDTTIRPTS LKVRLPISIK DLASEMKLKA SQLVGKLFLQ GIVVTLNDLL EDETTAQLLG QEFGCEITID TAEEKRIQIT DKSIREELQQ SPTDQLQLRP PVVAFMGHVD HGKTSLIDAI RKSNRAAGEA GAITQHIGAF RCHTTVGDIA ILDTPGHEAF SAMRARGADV TDIVVLVVAG DEGLRQQSIE AIQHARAANV IIVVAINKCD KPNFNPDNVY RQLAEQNLLP EPWGGQTITV NCSAVTGEGI PELLEMLALQ AEVLELRANP SMRARGTVLE SEMHKGLGSV ATILVQNGTL KRGDALVFGL LWGRVKTMHD EYGKELQEAG PSTPVEITGL SGLPEAGQEF IVVKNEKEAR EIANVRSEGA RQNTFMLQQK KKVSMENMLQ QASATGKKML NIVLRADVQG SLEALKVALL KIESDKADLN IIFNGVGEVS ESDVQLAAAS KAIVLGFHTQ IESHAEALVK QLGVQVRLHN IIYHAIDDIK VLMAGLLEKI AQETEKGKAI VKATFKSSQA GIIAGCQVIE GSIHRNNYVR LKRGQEVIWK GTISSLKRVK EDVREVQKGI ECGILLNNFT DILEGDIIEA YDITYISQEL //