ID A0A2I0MS44_COLLI Unreviewed; 1255 AA.
AC A0A2I0MS44;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=EIF5B {ECO:0000313|EMBL:PKK32500.1};
GN ORFNames=A306_00003015 {ECO:0000313|EMBL:PKK32500.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK32500.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK32500.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK32500.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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:PKK32500.1}.
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DR EMBL; AKCR02000003; PKK32500.1; -; Genomic_DNA.
DR RefSeq; XP_013223165.1; XM_013367711.1.
DR AlphaFoldDB; A0A2I0MS44; -.
DR STRING; 8932.A0A2I0MS44; -.
DR InParanoid; A0A2I0MS44; -.
DR Proteomes; UP000053872; 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 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 ECO:0000313|EMBL:PKK32500.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 664..881
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 64..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 142572 MW; F0C5712E3F8DD01E CRC64;
MWLYGNRRDD VEEAFNRYVF EKDRMVRLGV FCSGEFEGMR VRMDLEGHAK DDIDIDALAA
EIEGAGAAKE QEPQKSKGKK KKDKKKQDFD EDDILKELEE LSIEAQGGKV DREPSTGKVE
NDNEESLSKQ DKKRKGKSKK ANLENDYDSE EVEDKDKKSK KTQKAKQDML SGSDDDDHET
QLKKSKGKTQ KSNKKHDLLE EDETNIKKSK ERVVSSGESG DESDEVSQTR KGQKKTPKPK
STSAAESGDD EVEPSFKVKT VAQKKAEKKE RERKKREEEK AKLRKQKEKE ELEGGKEPAK
SKEAPKKAEE KASPEVMATP GPGEKGETPA GTEADDNEGD KKKKDKKKKK GEKEEKEKEK
EKKKGPSKAT VKAMQEALAR MKEEEERARR EEEERIRRLE ELEAKRKEEE RLEQERKERK
KQKEKERKER LKKEGKLLTK AQREARARAE ATLKLLQAQG VEVPSKDSVP KKRPIYEDKK
KKKQQQTENK EESVEVTSPA EDAVELEAPV KEEIPLPVEP VSEEKEEEEE TEDAGLDDWE
AMVSDEDVEK ESKPVHIEVK EQNEVEEEEE EEEDEEEEEE ESEESEDSEG SEDEDEKTSD
EREADSQAIG KQSVEKKPSK EISSDSEYDS DDDRSKEERA YDKAKRRIEK RRAENSKNMN
TEKLRAPVIC VLGHVDTGKT KILDKLRHTH VQDSEAGGIT QQIGATNVPL EAINEQTKMV
KNFDRENIKI PGMLIIDTPG HESFSNLRNR GSSLCDIAIL VVDIMHGLEP QTIESINLLK
SKKCPFIVAL NKIDRLYDWK KSPDTDVAVT LKKQKKNTKD EFEERAKAII VEFAKQGLNA
ALFYENKDPR TFVSLVPTSA HTGDGMGSLI ALLVELTQTM LTKRLAECQE LRAQVMEVKA
LPGMGTTIDV ILINGRLKEG DTIIVPGVEG PIVTQIRGLL LPPPMKELRV KNQYEKHKEV
VAAQGVKILG KDLEKTLAGL PLLVAYKEDE IPVLKDELIH ELKQTLNAIK LEEKGVYVQA
STLGSLEALL EFLKTSEVPY SGINIGPVHK KDVMKASVML EHDPQYAVIL AFDVRIERDA
QEMADSLGVR IFSAEIIYHL FDAFTKYRQD YKKQKQEEFK HIAVFPCKMK ILPQFIFNSR
DPIVMGVVVE AGQVKQGTPM CVPSKNFVDI GIVTSIEINH KPVEVAKKGQ EVCVKIEPIP
GESPKMYGRH FEATDILVSK ISRQSIDALK DWFRDEMQKS DWQLIVELKK VFEII
//
