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Database: UniProt
Entry: A0A165Q487_9APHY
LinkDB: A0A165Q487_9APHY
Original site: A0A165Q487_9APHY 
ID   A0A165Q487_9APHY        Unreviewed;       348 AA.
AC   A0A165Q487;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Translation initiation factor eIF2B subunit alpha {ECO:0000256|ARBA:ARBA00044208};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit alpha {ECO:0000256|ARBA:ARBA00044236};
GN   ORFNames=DAEQUDRAFT_727164 {ECO:0000313|EMBL:KZT68987.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68987.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT68987.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT68987.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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DR   EMBL; KV429061; KZT68987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165Q487; -.
DR   STRING; 1314783.A0A165Q487; -.
DR   OrthoDB; 51607at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1070; Translation initiation factor eIF-2B, N-terminal domain; 1.
DR   InterPro; IPR042528; elF-2B_alpha_N.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR45860; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR45860:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 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:UP000076727};
KW   Transferase {ECO:0000313|EMBL:KZT68987.1}.
SQ   SEQUENCE   348 AA;  37656 MW;  827524B8EA26B1B0 CRC64;
     MAGSQENADS DVCATYQRII QDEQLSPPLA AILTLTESIV KSNAGTMFEL VQALNDAAKV
     LKKQIPNSIS LNAGCELFIA FVTLFPHESD SFAELKTELV QQGQKYAAEA ISFRDKIAEA
     TLGFIKDDSV ILTHSYSRVV MKALLHAHKT KRISVFVTEA RPRGLGLKTH EALTAAGIPC
     TVVLDSAVAY VMDRVDFVMV GSEAVVESGG LINAVGSNQM AIIAKAANKP FYALAESYKF
     HRLFPLSQYD LPTHNPTILS FAALQRRPTP PDKFSHDTVA SGQSVARDGI SETGIAPPPT
     EMKMTTEQMS RNPSVDYTRP DLISLVFSDV GILTPEGVSQ YLVGMFAG
//
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