ID A0A1X1BK11_9APIC Unreviewed; 1525 AA.
AC A0A1X1BK11;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Translation initiation factor IF-2 {ECO:0000313|EMBL:ORM40459.1};
GN Name=infB {ECO:0000313|EMBL:ORM40459.1};
GN ORFNames=BXIN_1956 {ECO:0000313|EMBL:ORM40459.1};
OS Babesia sp. Xinjiang.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=462227 {ECO:0000313|EMBL:ORM40459.1, ECO:0000313|Proteomes:UP000193856};
RN [1] {ECO:0000313|EMBL:ORM40459.1, ECO:0000313|Proteomes:UP000193856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinjiang {ECO:0000313|EMBL:ORM40459.1,
RC ECO:0000313|Proteomes:UP000193856};
RX PubMed=27784333; DOI=10.1186/s13071-016-1846-1;
RA Guan G., Korhonen P.K., Young N.D., Koehler A.V., Wang T., Li Y., Liu Z.,
RA Luo J., Yin H., Gasser R.B.;
RT "Genomic resources for a unique, low-virulence Babesia taxon from China.";
RL Parasit. Vectors 9:564-564(2016).
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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:ORM40459.1}.
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DR EMBL; MBFZ01000058; ORM40459.1; -; Genomic_DNA.
DR VEuPathDB; PiroplasmaDB:BXIN_1956; -.
DR OrthoDB; 231149at2759; -.
DR Proteomes; UP000193856; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19757; Bbox1; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR000315; Znf_B-box.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF20; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:ORM40459.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000193856};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00024}.
FT DOMAIN 147..193
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 527..639
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 924..1105
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1274..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 168573 MW; 3E5DCBE84EFE6072 CRC64;
MTGFVLGDLN TPAMDLGRMI KTDGTDLFAG YIGAARERLP QLAETVVDTF GRVKDIFERP
MQLRKPEFDT EVLKPSRQVD LAETHRASDI EVKPVPKQRI NEDLRVEHLA DITKAQFDAT
QSNNLGKVNK LNTERRVTGL SASPCDIEAR LCSDCYLSLA TVRCDSCVTH FCGVCAVQRH
SDGINQTHKL VTATSGKEAR LTASDALCGD LSYGQMATQP SGSIVGNMYQ DLTIQIRPGE
SAFPSYDMCA VHSGLPLKFA CVHCHLLPIC DQCAKEAHVG NEHKVVEIES AVAEVKALLG
ECLGAVVRRH NDLSLVLPEL QQVSDTANAG LKNATRSIRG GLQRVLDALK LKRTLGMQDI
VNMQQVGSAA LNRLMHASGA LNKYLRGCVS QLEAINRIQN PGMALNMFVD LRANFEKMLF
TDEEIPDLVL EVPHWQLHCG NLPNLLSDHE SRLNSNFAQI SALASSLRRH VRETVSDIEQ
VSKGTSIGRN QPVVSQQVRR YAERRTRPAG PAVWVEGAEN TLDIVTHAEL KGLFLRRDSQ
RCVWRQRAVY LCGVRLFVME SDFFAEDVPV ESSIDLGAVT IRKFSDPDVL QITKLQRMGH
PNGFEVTEHN SGAMRYWLFT CESDKTVQLW VARLNQVAQH LQNERDAVTP HFKERERTDT
PQVGEAPPDA TLQMLHRVTC EPSTTGFVAD PEGEHRTCEE THDVEYMYDE QNFKLVAESL
RKIKNESKSL YNKCFRGDIE AEVGRLQVER ISHHAASLPL TESLSQADDA SICTSSPREN
VSRTERISVG RYAMPEMPLQ RSLSRWLSYR GRFLPLGRAA FRKTLLRGRA QRSPEILLPP
WVAVHELRLM LRVNYPACLR ACGVSVARGS YSWSDVEGRR FRTDNKRHVL VPFEAAAAAS
KNFGFQAIRV SPEPSTPQRC VDPRAIPVIA IVGHKDHGKT TLMERLSGEV FAAYELGNTT
QEVVIRSALL PTETEPLRAT LMDTPGDELF EMVRGRALHL ADVAVVVLSA EGGETQTRDL
ILQADRFRVP VVFCINKADL EFSDPEVARA ELRAQCLRMH SAGLISSGMV SNVEGAVAVS
ARTGACISSL GTGIVRTLAN VTLPVNPVVM KDCFGGVPLS EVESFIRRTN CLVSTGAPPI
AICFILEVER THSFGVVLTV VIRHGVLIEG GYFVAGTEYG RVSGIYPSYG RIAPDTKVER
ATVGHAVRVT GLKTVSGTSA DDLLLTLPQH EAFRLSQYRR DIQLLRANQL EGPPIDLPWA
VLLKSKEDVG YDQDTTTTAS SLDGENTSDV ADSGDDVEEL GTVSTSIYLR PIDDDMVESS
GDLEAELCAT ETDKEIPSSP SDSASREQER YEENTPHEAW VAEVAQRNAE LQNRWRVNLN
RVEPSAKVPK AHGVISPPKV TLEMGRPVIP VILRANFVGS FDALLDGFED LERKYHVRIP
VVHGGLGAVA PNDVVQADVG NKFGYCPIYA FQVPVLTDAA KHAVINHVTV KQFNVYSDLL
ADVEKRCERA VRLANEARER EFLTK
//
