ID A0A1W5D7R6_9LECA Unreviewed; 1610 AA.
AC A0A1W5D7R6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM39081.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC of dynamic microtubules. Required for mitotic spindle formation.
CC {ECO:0000256|ARBA:ARBA00024889}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000256|ARBA:ARBA00011375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
CC -!- SIMILARITY: Belongs to the CLASP family.
CC {ECO:0000256|ARBA:ARBA00009549}.
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}.
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DR EMBL; FWEW01003312; SLM39081.1; -; Genomic_DNA.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
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; IPR034085; TOG.
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; PF12348; CLASP_N; 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 SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:SLM39081.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1016..1234
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 101..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1610 AA; 176207 MW; 35341C4EB4B94CA6 CRC64;
MAAPINSLVE KAFVALINVA VLYLWSPYLC RFLLVVYMSK KYMELCSATS DSSTSSSLST
SHAEDLPVSL SSSHAGVLPV ALSTQHAEDL PVVDVVMSGK DPKHVGGTRA APSHTKTHDR
IPSTDSKLPL APSPSPTAED TDQIKPLHLN TRQELEDIFR IMSPYFEGKE SEQNWTHREE
SVIKLRSITK GNAPTEHTTT YLAGVKGLLD GIVKTTNSLR TTVSTNGCHL VRDIAKAAGP
GLDPMVEILL QNLIRLCAAT KKISHQNGKI TVDTIFTYAT YNVRLVQHIW NACQDKNVQP
RTFAAEWLKT IIARHGHHKH VLEHGGLDLI EKCIKKGLTD ANAGVRTSMR PTYWAFWRVW
PDKAEAIMSS LELKQQDQLR GDAANPTPVT LTASKKAPPP RATTSRPSLK ETMAAKKRSA
PAGKDLPETS AATTKAPTAP ALTLLSTQGP SHQRAFMNDD DLYVHATNYQ DLLSAQTTAQ
FTYESVKMPP KKKGNKKGND DWETELGESM DPIAAATQDA KEAEVAQDAE EDGAANAGGG
LLAALKKNKS KKQKKGKQVD EDYVASEDPP AANGANGHAA FDGIDDLAAK APEEATTEDL
FEVQTNKTKG GKGKQGQAKI KEEEEESAEE EGSTLKSKKE KEKEKKEREK QRKKEQAAAK
KKTTTAPAPP PKAEPTKPVP EAKPEPTSAV DAGKGKKKVP AALALLQKQQ EAKKKKEEEE
ARLAAEEAAR IAEEERLAAE EEKRKEEARA RKKEKEKEKK EQLKREGKLL TPAQKALQER
NELRKKQMLE AGAKVAGLQD PAEKKKPVYD NKRRKGFKKP GDDARLEEEK AAAEAGARRQ
VEAEERLRLD EEAKAKAEAE AAAEAAKKEE SDGLDDWEAV ADADADVKDS WDAETDEEDE
QSEPKAVDGK LTNGQAKITP SAVPTKSSDE SQLNKSGVKG AKLASETAKG VSKAPVRTQS
KLQNKDDESD SDSDDSSEDE GATATQRAAA QKKAEAAARR KQQHEEALAA RSKDNLRSPI
CCILGHVDTG KTKILDRIRQ TNVQEGEAGG ITQQIGATYF PVEALQAKTQ VVNKDGSFEF
KVPGLLIIDT PGHESFTNLR SRGSSLCNIA ILVVDIMHGL EPQTLESMKL LRDRKTPFIV
ALNKIDRLYG WKKIDNNGFQ ESLALQNKGV QNEFRDRLEK TKVAFAEQGF NSELYYENKS
MARNVSLVPT SAHTGEGIPD MLKLIVSLTQ ERMTNKLMYL SEVECTVLEV KVIEGLGTTI
DVVLSNGVLR EGDRIVLCGL NGAISTSIRA LLTPAPMKEL RIKSQYVHNE EVKASLGVKI
AANDLDNAIA GSRLLVVGPG DDEEDLEEEV MSDIENLLGK VSKTGRGVSV QASTLGSLEA
LLEFLKVSKI PVANISIGPV YKRDVMSAGI MLEKAKEYAV MLCFDVKVDK EAQAYADEVG
VKIFTADIIY HLFDDFTKHM AQLAEQKKED SKLLAVFPCV LTPVAVFNKK DPIVIGVDVT
EGNLRLLTPV AAVKTNPVTG VKEVVSLGRV QSIERDHKQI PICKKGQPSV AVKIEGPNQP
MYGRQLEEKD VLYSLISRQS IDTLKEFYRA DVSNDEWALI KKLKSLFDIP
//
