ID A0A225AIT4_9EURO Unreviewed; 1320 AA.
AC A0A225AIT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Translation initiation factor eIF2B subunit epsilon {ECO:0000256|ARBA:ARBA00044144};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit epsilon {ECO:0000256|ARBA:ARBA00044345};
GN ORFNames=UA08_03810 {ECO:0000313|EMBL:OKL61361.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61361.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL61361.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61361.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000256|ARBA:ARBA00007878}.
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:OKL61361.1}.
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DR EMBL; LFMY01000004; OKL61361.1; -; Genomic_DNA.
DR RefSeq; XP_020121482.1; XM_020266151.1.
DR STRING; 1441469.A0A225AIT4; -.
DR GeneID; 31003565; -.
DR OrthoDB; 5474157at2759; -.
DR Proteomes; UP000214365; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd04197; eIF-2B_epsilon_N; 1.
DR CDD; cd05787; LbH_eIF2B_epsilon; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16625; RING-HC_RBR_HEL2-like; 1.
DR CDD; cd11558; W2_eIF2B_epsilon; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035543; eIF-2B_epsilon_N.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR003307; W2_domain.
DR InterPro; IPR044123; W2_eIF2B_epsilon.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45887; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR PANTHER; PTHR45887:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00483; NTP_transferase; 1.
DR Pfam; PF02020; W2; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS51363; W2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 537..709
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT DOMAIN 933..1147
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 937..986
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..731
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..833
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 148540 MW; 50A1F390548033FA CRC64;
MGPKQKGGSG GGGGGASKHK GNTAEEVEET LQAVVFADTF ETRFEPFTLE KPRCLLPLAN
TPLIEYTLEF LANAGVQDVF LYGGAHSNIL EKHISTSRWK APSSPFKKLT FLKSTSTSVG
DVMRDLDGKH LITGDFIAVS GDVISNFPID EVLAKHKARR QTDRNAIMTM VLREAGAQHR
TKSSSISPVF VVDPTKDRCL HYEEIDHHHH DTSLSPPARL TIDTEILTSQ AELDIRQDLI
DCNIDICTPD VLSLWSDSFD YQAPRKHFLY GVLKDYELNG KTIHTHIIKE HYAARVRNLK
AYDAVTKDII SRWTYPLCPD TNLLPGHTYE LRRGSIYQEQ GVILARSCIV GRRTVIGQGT
SIGDRTTVTN SVLGRNCKIG KNVVLDGAYI WDGAVIGDNT EVRQAIVAEG VVVGDNCKVE
PNVLLSFGVK ISNGVTVGEG TRVTVAARED GSVPANEEKI VGAQGRGYEY VLEEEDEEDE
EDDRSEASGL VYNMAKLSLS TDSISTLSSE ISADDDYSHG QRSDSFGTLV SEDEDHDHFQ
HDASNNLYDS IRDGVSADVV ALELVSLRMS ANASDYQVRR AVASSFMKRI SQLVTEAGKG
AGDAVHEVFS RYKDVVERSL FDKNKEQKTD QIDLLLQIQQ DLVHRAKGDT ILLFTAKELY
DLDIIEEEAF EGWWADERSS STEEMKKVRA QTQQFVDWLA NASEEDDDDD DDDDDDEDGS
EDEDEENNDD DDNNNNYNHR SASAAKHHKA LPLERSVQGK RQPSPAPGTR KAEVDKDLAP
LSLSKQGASI VTPTTTTRSM DSDDDFMTDV SSREEDFLDT QDSDDESLGE DFGDEFDNGF
SYDKDLVQKT KKPYEVDFTV LSPADIDREQ NYQITEVSSV LGLPPESSGI LLRFARWNRE
KLIESYMDRS EELLEEAGLG HSFDVNPRTD TVPGFMCSIC CEDDEDLETY AMRCGHRFCV
DCFRHYLEQK IKEEGEAARI QCPQDHCHRI VDSKSLNLLV SDDLKYRYKT LLTRTYVDDK
DNLKWCPAPN CEFAIDCGVK ARDLNKIVPT VHCSCKHSFC FGCGLNDHQP PPCSLVKMWL
KKCEDDSETA NWISANTKEC PKCLSTIEKN GGCNHMTCRK CKYEFCWMCM GLWSEHGTSW
YNCNRYTEKS GSEARDAQAR SRASLERYLH YYNRYANHEQ SAKLDKDLYL KTEKKMTSLQ
SQSGMSWIEV QFLDTASQAL QQCRQTLKWT YAFAYYLARN NLTEIFEDNQ KDLEMAVESL
SEMFEKPIAE LAELKVDILD KTAYCNKRRV ILLSDTAENL KQPHDSSQFV FVPVCSSNHV
//
