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Database: UniProt
Entry: A0A0A2KCX6_PENIT
LinkDB: A0A0A2KCX6_PENIT
Original site: A0A0A2KCX6_PENIT 
ID   A0A0A2KCX6_PENIT        Unreviewed;       434 AA.
AC   A0A0A2KCX6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Translation initiation factor eIF2B subunit beta {ECO:0000256|ARBA:ARBA00044122};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit beta {ECO:0000256|ARBA:ARBA00044228};
GN   ORFNames=PITC_052860 {ECO:0000313|EMBL:KGO64741.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO64741.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO64741.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO64741.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
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:KGO64741.1}.
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DR   EMBL; JQGA01001564; KGO64741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KCX6; -.
DR   STRING; 40296.A0A0A2KCX6; -.
DR   HOGENOM; CLU_016218_4_3_1; -.
DR   OMA; SHSCAVA; -.
DR   OrthoDB; 169494at2759; -.
DR   PhylomeDB; A0A0A2KCX6; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR45859; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR   PANTHER; PTHR45859:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR   Pfam; PF01008; IF-2B; 2.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000313|EMBL:KGO64741.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:KGO64741.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   REGION          115..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  47285 MW;  8F6D518D22DD810C CRC64;
     MPSSSLALTP GLGSFLKCLK TNPIDTSIET LISLLKRRQI RHSRSCATAT AYLLRSVISA
     CRTADSAKLI ERVQSVGRRL MAAQPREMVV GNIVRRVLGL IRDEAEDDRD AEFALSDIGS
     ESQPQTPRAY DDPSLPLDRD SLSFRSEERS SRPPLTSMFS LLSHPEPENS LPSTPGSSSP
     NGRLPGHGPS KDVRAEVLEG IGEIIDELGQ VDDQIAAYAL DHIHSNEIIL THTSSTTVQK
     FLLKAAAKRK FTVIHAESYP NNHEATHATI SGSAVSDDDN LGLEAFQKPL IEHGITVILI
     PDSAVFALMS RVNKVILGTH SVLANGGLVA AAGTRVIARA AKVHQTPVVV VSGVYKLSPV
     YPFDFDSLIE YGDPSKVLPY EEGDLVDLVD VQNPIYDYVP AELVDLYITN LGGHAPSYLY
     RIVSDHYRKE DISF
//
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