ID A0A2G5UNS7_9PELO Unreviewed; 1114 AA.
AC A0A2G5UNS7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN Name=Cni-iffb-1 {ECO:0000313|EMBL:PIC41001.1};
GN Synonyms=Cnig_chr_III.g8572 {ECO:0000313|EMBL:PIC41001.1};
GN ORFNames=B9Z55_008572 {ECO:0000313|EMBL:PIC41001.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC41001.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PIC41001.1}.
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DR EMBL; PDUG01000003; PIC41001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UNS7; -.
DR STRING; 1611254.A0A2G5UNS7; -.
DR Proteomes; UP000230233; Chromosome iii.
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 CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 490..711
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 125632 MW; AA44643DA3E640FE CRC64;
MPPKKGGKKN KDDDWDDDAA EKKLAALNIG GASETNWDDE EPKKAKAKAK APAKKGFAAF
LDEDSEPEQK PSDDDEPAAP VKEAIPAPKK EKKEKKKGGK KGKKEENDDE DLDALLASIE
NAPAAAEVAA EEEGKNKKDK KKKKEKAPEP AEEPKKSTSE APEASPETPE APEAPESSEK
AEPAEEGGDD KEKEKKDKKK DKKKQKEKEK KEKEKEEKKG KKEKGTLSMI KEMLKKQQEE
REEQERLQKE QQEREAQEEL ERQERVKAEK ERKEAQKEAK KAEIERQKAA GTYVTAAQKR
QQALALEKLR AAGYTVPAPR DSTEEEGAPK KSFVYVDEKT KAKQEEKKRR RLEKLGQLPV
EEVKEEEKVE TPESPEAVTP DQEKKELTPE PLDDWEMADS GDEEKEEEKK KPEKKAGAAV
VKESVDEEES SEEEESDEET SEEEETSEEE EEEEENRGQR ETKEQIMERV RARIAKRKEL
AASKKSTDDL RSPVICVLGH VDTGKTKMLD TIRRTNVQQG EAGGITQQIG ATEVPAEAIK
ERCRQVRGFL QDQMKIPGFL IIDTPGHESF SNLRTRGSSL CDFAILVVDI MHGLEPQTIE
SLKLLIKGKT PFVIALNKID RLYEYESNPR KDVYELLKSQ KPRVQAEFKE RMDKIIVEFA
EQELNVTLSN SKKAEDSDYV CMVPTSAMLG DGIGNLMAFI VNQTQTKYAQ KLAFSEELDA
TVMEVKQIAE KFWILNPEDV RISNSLKLGQ YGYQNDGNFK PSLGTTIDVI LVNGTMRAGD
VLVLTGTNGA IVTQVRELLM PKPLKDLRVK NDYIHYKEVK GARGVKVLAK DLEKVLAGLP
VYITDQVDEI DYLRQEADNQ LANALHAIKK KPEGVYVQAS TLGSLEALLD FLKSQKIPYS
NVNIGPVHKK DVQKASAMKE HKAEYACILA FDVKVEREAQ IFADHEGVKV FQADIIYHLQ
DAFLKYREEL KEKARRENEH LAIFPCKLRV LPNHVYNTRN PIVFGVSIEA GQVKRGTPIC
VPSKEGLLLG TISSVQRNNE EVPLGKQGEE VCIKIENTTG EAPKLYGRHF THEDPLVSKI
TRESIDVCKT YFRDDLTKAD WQLVVQLKKM LDIM
//
