EI2BD_SCHPO
ID EI2BD_SCHPO Reviewed; 467 AA.
AC Q09924;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable translation initiation factor eIF-2B subunit delta;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit delta;
GN Name=tif224; ORFNames=SPAC21E11.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-19; SER-21; SER-23;
RP THR-27; SER-28 AND SER-37, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP. {ECO:0000250}.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA91965.1; -; Genomic_DNA.
DR PIR; T38138; S62591.
DR RefSeq; NP_594503.1; NM_001019932.2.
DR PDB; 5B04; X-ray; 2.99 A; G/H=1-467.
DR PDB; 6JLY; X-ray; 3.50 A; G/H=1-467.
DR PDB; 6JLZ; X-ray; 3.35 A; G/H=1-467.
DR PDBsum; 5B04; -.
DR PDBsum; 6JLY; -.
DR PDBsum; 6JLZ; -.
DR AlphaFoldDB; Q09924; -.
DR SMR; Q09924; -.
DR BioGRID; 278541; 4.
DR DIP; DIP-61961N; -.
DR IntAct; Q09924; 3.
DR STRING; 4896.SPAC21E11.06.1; -.
DR iPTMnet; Q09924; -.
DR MaxQB; Q09924; -.
DR PaxDb; Q09924; -.
DR PRIDE; Q09924; -.
DR EnsemblFungi; SPAC21E11.06.1; SPAC21E11.06.1:pep; SPAC21E11.06.
DR GeneID; 2542064; -.
DR KEGG; spo:SPAC21E11.06; -.
DR PomBase; SPAC21E11.06; tif224.
DR VEuPathDB; FungiDB:SPAC21E11.06; -.
DR eggNOG; KOG1467; Eukaryota.
DR HOGENOM; CLU_016218_3_0_1; -.
DR InParanoid; Q09924; -.
DR OMA; YIDMVIT; -.
DR PhylomeDB; Q09924; -.
DR Reactome; R-SPO-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q09924; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:PomBase.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:PomBase.
DR Gene3D; 3.40.50.10470; -; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..467
FT /note="Probable translation initiation factor eIF-2B
FT subunit delta"
FT /id="PRO_0000156071"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6JLZ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6JLZ"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6JLY"
FT HELIX 186..204
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 231..248
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 415..421
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:5B04"
SQ SEQUENCE 467 AA; 51583 MW; 3C7029EBDFEF6EAF CRC64;
MGFSAEQAKK DGKDQSPVSE SSSVGGTSPA TASSVVSPNE PKLSGKEAKA LKKARKQASR
RAKAEAAAAN NPPGVSEEKK VAIPNKNSNQ QKKASKQNPQ NSPETDANLQ EKKIFEEKQV
SIFSHLDWRR RRTTENIPKD IHPAVIRLGL KLANYKIFGS NQRCIDLLKT FKIVIQDYQT
PYGTTLSRHL TTHINSQIAY LVSTRPLSIS MGNAIRFLKL EISVLDIDLT DDEGKELLLE
KIDSYIRDRI IIAGQVIVQA ATEKIQDGDV ILTYLHSSTV NDVLIHAKNV GKKFRVVVVD
SRPEFEGRVC LKLLTEHGIE CTYVMISALS YIMQEVTKIF LGGHAMLSNG ALYSRAGTSL
ISLLGHESNV PVIACCESYK FTERIQLDSL VYNELAPGDQ LVNMGVDDFE EKPGVLANWK
SVKNLKLLSL KYDVTPPRLI TVCVCEMGLL PSTSVPAIIN EFKQVYA
