ID A0A0V0VQ62_9BILA Unreviewed; 1387 AA.
AC A0A0V0VQ62;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819};
DE Flags: Fragment;
GN ORFNames=T09_7687 {ECO:0000313|EMBL:KRX65537.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX65537.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX65537.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX65537.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000256|ARBA:ARBA00003993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00649}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC {ECO:0000256|ARBA:ARBA00009573}.
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:KRX65537.1}.
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DR EMBL; JYDN01000016; KRX65537.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0070449; C:elongin complex; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro.
DR Gene3D; 6.10.250.3180; -; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF06881; Elongin_A; 1.
DR Pfam; PF08711; Med26; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KRX65537.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649}; Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 1..77
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX65537.1"
SQ SEQUENCE 1387 AA; 154152 MW; 1CB69982F76AFC4C CRC64;
LKMNYKDEIE GLKKWLLGDD RVKKMRALRK LETLPITLEI LQQTGIGIAL NSLRNEKEYS
ERVKTLVFKW KEIAYSTARK KGIEIDFCET TANKYSVKPR DATVAESAVK ITSSSSSKVS
TKPDTLAKCE MKRSADTRST EDALTSEKES ASAFKVPKVS KRIKLTTGSD SFADALGSVD
HLPKNYNRSH KRKLGQKSKQ IPNGDSLPDV EILKSLQTSL NEPGPSNQSN MYSVKADSKP
PSYNKPKTND CAIKKSCTMK GDYDYLDQQL VKRGHSRTQV YSGRRSHIVQ SIQKLFDMCI
RVLSDNIDQL EFTGGVPYSI LRPVLSRASP QQLVKIEHYN PYLSIDLQEL WKEHCKKEFN
CLACDLLKKE TYRQMYERMV MQREQKFLEV TRSISESMNN ANVRVAKLSE VKTPRDVLRR
QAKYGTGLLA LPSCEDIIES RRYGLAGGGS SSKMKSVRSA GIIVSSLRDQ SSKLAKPPLL
QNTARRTEAG HAALIGQFVR AELQAQYAVA FSGHLFGHLL ASGGFENHIP LLGKAAAAGL
GGEFVRTGEP GNLSGTTTQL FFGKIQPFGF DGCLEIYANQ STHSSHGRRV GHAGLTGENV
RARLERDVLF TATVFGQPTT DQRALVPPAS DDHLTAALGG EFVAAGLHGY DGVGLVAPVV
TLTVGQQPVL LVLDSADVGS AGEERRRALL RGELVGSALG SGDALALAVR LDEAAVFGPV
YVRPRTAESA HPFLRGEFVG AGLQRQYRLA GVELFKSPLA RFGRTKCGII PLNDKDPFGV
GSGRIVPLAH SHRPIECLPT PKNPNLGVFR IRDDKSITVY AGVSNPVQVF NFECRACTGG
ATLTFSNDGK YFAFCDEKIF VYKCSKWRLH AAFDENEATN LFFSPKNSVL CTFKPYSTAV
GVTSVESNLK LWSMFTGELL CEWVQKNIVS WRPMWTADES IVLRLVGSEL WFIAPENLNR
FVQKLTLPKL TSFSLSPGPA PFHVAVYTAS SNEKMASARL YRCSLKAPID IIACKNFQAD
RVDFHWNKNG TAVLVMAILD VDPQNKSYYG CENLHLMTTY GEACNVPLDR EGPIHSVDWH
PGSKLFCVVY GYIPSKAALF DLKANRVCDF GCEPRNEIEK KSLNSLLKIR HFLKSLPTAF
TSSPLPRLHV CALKIWHCSG KVIHEINCID ETLLWQVIWS SEGKDKFPKP VIDLSSFQGA
KAAEPAKSSL GEVDSRFNGD ESASKKKKNV GFKKDHHGNF GKLLNTVNTK ATDKGERMKK
IRSLQTKLRQ IKILKDKQSQ GCKLELNQIE KINREEEIQA QLEQLTITGG ATRLKEKEND
RDRKTVVMFC FAGARVGWRF VIFPRKASSL PSHKNQKHRD EQNGRGDDRR ELPPLHADLV
RNGFAFH
//
