GenomeNet

Database: UniProt
Entry: A0A176VVP8_MARPO
LinkDB: A0A176VVP8_MARPO
Original site: A0A176VVP8_MARPO 
ID   A0A176VVP8_MARPO        Unreviewed;      1601 AA.
AC   A0A176VVP8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, 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};
GN   ORFNames=AXG93_4242s1090 {ECO:0000313|EMBL:OAE24837.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24837.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE24837.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24837.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) 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:OAE24837.1}.
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DR   EMBL; LVLJ01002459; OAE24837.1; -; Genomic_DNA.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000077202; 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   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          943..1158
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..786
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..814
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..913
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1601 AA;  175457 MW;  01AE0A15CDBC7FC6 CRC64;
     MGRKKPTSAA VDEFEPDSAS VAQAPSGNAK KGKKKGAVKV DDDEYMVEPA VEESVNGEQE
     RGSGDLEADL ADQLQDLSFS GKKKTKGKNA KKAELDSSDV SFQQADETSL EEFVGGSKKK
     GAKKGKKGNR VDDDEYEVSE SVDVESTPSE VPSFAEESGA GNKKKGKKGK KGTKGDDDDF
     DVEISEPAIS VQSEDFGAKK KGGKKGKKGG RIDDDEYEIP ELVESEQVAP VEPEEPVFSG
     KKKAGKKGKK GAKVDDDEYE LQPTIEAPAQ LDETPEPEEP IFSGKKKAAK KGKKGAKLDD
     DEYELPGSNE AGSEDPMVID ELEAPKKSEK KAGKKATSTK PADLLSLLAG LDEGSVEAGD
     EDAEERTAPQ STQKENGDLS GDEVVFSGKK KAKGKKAPKV IVDDEITNGG GLDANAGLRE
     EASVYVEVEP EVDDEVIAFS GKKKPKKGKK EVKKDVEADD MGETAELPSL PTVSSPPVEP
     SPSVTESSSS SKKNKKKGKK SGRTAQEEED LDALLAELDG PVMSKAPPKS AAPSETPAES
     QPIEEQPADE VVPEAPAVAE GEEVVESAAA KKKKKKKEKE KAAKAAATEK PVDEEAAESA
     KPKEEAKGKA AEKKIPKHLK AMQEQLAKIR EAEEKRKREE EERRRKEEEE QARLEELERQ
     KEEAKKRRKE REKEKLLQKK KEGKLLTGKQ KEEARRLAMM REQMLAQAGI AVDSIDGAPV
     DAAPAAPRKP KYDSKKKKRG PNISQQSEQA ADLTKQEISD APIEEVEEVE EVPVEVPMEV
     EVAVEEEVAA PEPPPEEKSP EPEEEEEEED WDAKSFEDVA LPAIKSAFAE DEELDKRESL
     VVAPVPGKST KRVVAQAPAP PAKRAASPEK RPTPAPKRGQ QPHKGPHKAA PPPAESEEEE
     TESEEEEESE EEDDADTKKK RLAKDKREAR KAEALSKRSA DDLRSPICCI LGHVDTGKTK
     LLDCIRRTNV QEGEAGGITQ QIGATYFPMA NIRERTKELK AVAEMRVPGL LVIDTPGHES
     FTNLRARGSS LCDIAILVID IMHGLEPQTI ESLKLLQMRK TPFIVALNKV DRLYDWKSTT
     NAPIRNSMKN QSKHVIQEFE TRTNQIITQL KEQGMNSELY YKNKEIRKVV SIVPTSAISG
     EGVPDLLMLL VQLTQKMMEE KLMYVAEVQC TVLEVKVIEG LGTTIDVVLV NGVLHEGDQI
     VVCGMQGPIV TSIRALLTPH PMKELRVKGS YEKHKELKAA QGIKITGQGL EHAIAGTQLY
     VVGPEDELED IKEEAMQDMK NVMSRVDKTG EGVCVQASTL GSLEALLEFL KSPAVKIPVS
     GINIGPVHKR DVMRASVMLE RKRKEYATIL AFDVKVTQEA KELADEVGVK IFTADIIYHL
     FDQFTNYINT VKEEKRKETA EEAVFPCVLK LMPGCIFNKK DPIIVGVDVV EGIAKVGTPL
     CIPSREFIEI GRIASMEVNH KVVDTAKKGN TVAMKIVGTN AEETQKMYGR HFDMEDEFVS
     SITRKSIDLL KENYRDDLTM EDWRVKSLPD KVCEGCGGLA GIVLLVPVFC DSVRAKASLT
     PELIWVDSYE SFAVGVFCSH FFVGFLFRKV NLSPCNLVLE T
//
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