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Database: UniProt
Entry: M3N523_HELPX
LinkDB: M3N523_HELPX
Original site: M3N523_HELPX 
ID   M3N523_HELPX            Unreviewed;       464 AA.
AC   M3N523;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Translation initiation factor IF-2 domain protein {ECO:0000313|EMBL:EMG91325.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF1399_01569 {ECO:0000313|EMBL:EMG91325.1};
OS   Helicobacter pylori GAM118Bi.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1159027 {ECO:0000313|EMBL:EMG91325.1, ECO:0000313|Proteomes:UP000011879};
RN   [1] {ECO:0000313|EMBL:EMG91325.1, ECO:0000313|Proteomes:UP000011879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAM118Bi {ECO:0000313|EMBL:EMG91325.1,
RC   ECO:0000313|Proteomes:UP000011879};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA   Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:EMG91325.1}.
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DR   EMBL; APDD01000090; EMG91325.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3N523; -.
DR   HOGENOM; CLU_737258_0_0_7; -.
DR   Proteomes; UP000011879; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR006847; IF2_N.
DR   Pfam; PF04760; IF2_N; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000313|EMBL:EMG91325.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:EMG91325.1}.
FT   DOMAIN          375..425
FT                   /note="Translation initiation factor IF-2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04760"
FT   REGION          61..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          310..340
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        91..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         464
FT                   /evidence="ECO:0000313|EMBL:EMG91325.1"
SQ   SEQUENCE   464 AA;  53296 MW;  95C430A8EA2BA46F CRC64;
     MSDMVDLKKF VTELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
     IQANQPTKNP EQDNKDDLDT AVTPKSLNKK VSKTPKKEET KSQPKPKKTK EKKKEALTPI
     AKKKGGIEIV NTFENQTPPT ENTPKAVSHS QIEKAKQKLQ EIQKSREALN KLTQSNTNNA
     NSASNVSNAK KEISETKKQE REQEIKRHEN IKRRTGFRVI KRNDETENET ENSVTESKKP
     TQSAAAIFED IKKEWQEKDK QETKKTKKPS KPKATPTAKN NKSHKIDFSD VRDFKGNDIY
     DDETDEILLF DLHEQDNLNK EEEEKEARQN INDRVRVQRK NPWMNEGGIK RQSKKKRVFR
     NDNSQKVIQS AIAIPEEVRV YEFAQKANLN LADVIKTLFN LGLMVTKNDF LDKDSIEILA
     EEFHLEISVQ NTLEEFEVEE VLEGVKKERP PVVTIMGHVD HGKT
//
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