ID V2Y8F5_MONRO Unreviewed; 1185 AA.
AC V2Y8F5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Eukaryotic translation initiation factor 5b {ECO:0000313|EMBL:ESK87959.1};
GN ORFNames=Moror_10873 {ECO:0000313|EMBL:ESK87959.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87959.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK87959.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87959.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK87959.1}.
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DR EMBL; AWSO01000718; ESK87959.1; -; Genomic_DNA.
DR RefSeq; XP_007852739.1; XM_007854548.1.
DR AlphaFoldDB; V2Y8F5; -.
DR STRING; 1381753.V2Y8F5; -.
DR KEGG; mrr:Moror_10873; -.
DR HOGENOM; CLU_002656_4_0_1; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000017559; 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; 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; 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; 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:ESK87959.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 586..804
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..549
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 128945 MW; 7DE335E1EEB2854E CRC64;
MAPKNKGKKG KKADDDDFWE KAGESVANNN LSVPAGDASD DDSKPAKKSG GFAALMTEDT
GAAAEEEEDF GGLMSAIKAS SKKKEKKKTK KEAPPVDFDD EPAAEDAATA SSRKPVEMTA
EELADEEWGP VKEKGKKGKK GKGKKGKVEE PADDEEDDPS SKAATAPPPK EDGEDDGEDD
GDDAGGEVKI LSKKEKEKLK KEREKAKKKA QAAAKKAAEA ETPAAPTEQP PPPAAAETKA
EDNDEEADEA DAKSGSKKKK KKKAKKDDEP APAPAPAAGA KKKGGISALK AMMEEKKRLE
EEARRAEEEE RRRIEEEERK AAEEEKRKEE EKQRRKEKEK AKRELAKKEG RLLTKKQKEE
RAAAEMRKQA LLASGVQVEG LQQGGGQSAK KVNYGARKKK GPAAKDSSPA PESRPETPAP
ATPVIAEKFL EPQKPGNGTE KDDWDASSEE EQVAKPATTD VKDSWDASSD EEEEKPAAPS
VKAANGTAKT IPTSKAPETE AKEATPTANV KPAPSSKAAE EESEEEEESS SSDSESSSDS
SEEDSDSSDE ELSKAQKMAA QRKAEAAERR AKAHEAALAA RNKDDLRSPI CCILGHVDTG
KTKLLDKIRQ TNVQEGEAGG ITQQIGATYF PVEAIKTKTA VVNKDGKQEY KVPGLLVIDT
PGHESFTNLR SRGSSLCNIA ILVVDIMHGL EAQTLESLRL LRDRKTPFIV ALNKIDRLYG
WQATPDNAFQ DSLAKQTRSV QREFEDRVQK TTLAFAEEGL NAVLYYENKN FARNVSLVPT
SAHTGEGVPD MIMLLVNLTQ QRMSDRLMYL SELECTVLEV KVIEGLGTTV DVVLSNGILR
EGEKIVVCGL NGPIVTQVRA LLTPQPLREM RIKGAYVHHK EVKAALGVKI VASDLEKAIA
GSRLLVCGPD DDEDDLRDEV MSDLTSLLNS IDKSGRGVCV QASTLGSLEA LLDFLKVSKI
PVSGINIGPV HKKDVMRAAT MLEKARELAC ILCFDVTVDK DAERMAEEMG IRLFKADIIY
HLFDKFTAYN AEITEAKRRD AAPQAVWPCR LKTIAAFCKR DPIILGVDIL DGSLRVGTPL
AVVKVDPVTQ KKEIIDLGKV TSLEINHKAH DVVKKSQAGA GVAVKIEHAV YQSAKMFGRH
FDDKDEIMSH ITRQSIDVLK ASFRADVSNE EWALIKALKP RFNIQ
//
