ID A0A0G4MJA3_9PEZI Unreviewed; 2217 AA.
AC A0A0G4MJA3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000256|HAMAP-Rule:MF_03000};
GN ORFNames=BN1708_006288 {ECO:0000313|EMBL:CRK34145.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK34145.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK34145.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK34145.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000256|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; CVQH01022861; CRK34145.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MJA3; -.
DR OrthoDB; 2475704at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 1.25.40.860; -; 2.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR002889; WSC_carb-bd.
DR PANTHER; PTHR14005:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A; 1.
DR PANTHER; PTHR14005; EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF01822; WSC; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00088; PINT; 1.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00321; WSC; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR PROSITE; PS51212; WSC; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03000};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2217
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002567454"
FT DOMAIN 35..126
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 138..234
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 1490..1674
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 281..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1745..1833
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 281..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1966..2064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2217 AA; 245058 MW; 8724F9692B983A12 CRC64;
MAPIKAWAAF AALSLVSTAH TWHVELPPCV NNFQPFVNSG CYANPDGKSL TYRSSTSSRE
MTVEKCTAEC KGNGYRYAGL EYYGVCYCGN TVNGAELAAG ECSFPCNGDK NETCGGDRKL
SVFEDRTFPA TDAVTIENYV DTGCWTDHSQ IGKSLSWPQD QLDKSVMTPS LCTEACRQGG
FPYAGVEYGQ ECWCGAVMGN ETRSVDASQC GIACKGDKTK TCGGRSRINI FFAKEFQSLE
PCGHQPQPPL SSAPVSSPAV TTSTLVSSSL TIVSSSLPLS SPASSTEVSS SHPYLEPSSS
SSSSSSSSST ASSSSASSSS TSSSSSTSSS SSSTSSSSSS SSTSSSSSTS SSSSTSSSSS
SSSSSSSSPA SSSSSTTTTS SPSSTTTPCT TTTLISSTTS TQAPPPPTTT APLTTTSTKS
PAICTTAVVT PPKHEYCCGN WCSTPIPDFG DWDTCAKAKA KCGLQVAACL KQAGWPGAIE
CFNFQQWCQN IDMFCGWMCR EGWDRSCSKK DYFNFYKPVG DGKPITSTST FPCAATTTTT
VPPATTTAVV PPPKGICIQP SNPWYGYGPG NPVGKIPLPA VTCNDLEHEF KGGXSYTRPN
VPSACADACR QQYDSCNAVY AKGCWSFKNW RNRREIGASH EVPVSAALAD RSPNLDAAID
KRTFGRFFGD SFWDATNKCK AQYDDCINVN RGVTGAGVCW FYGKCMHPPP QQLKASLQSM
PATGDACCTC AVLLATAPRY TSGSEKPLSE PRALPCCNRT ICGSCLYTNA RFALYCPYCQ
TSTAAALLPS GLRTTRDKSS VVLPPRTSSS STPSPPPPVL EEKVDDTIHH LDHATDTLTS
LSLAYNVPAQ VLRAHNNLPA DQLLPARRTL RIPASHYPAG SPSLSPHPVE SADEIRRKAA
LRRFMVACKV ADYDVATLYL EQAGHDLRAA VESWEADAAW ERAHPQESSG LGRKGKETRA
LRNARPLPNY AKTENFFILR GNHECASINR IYGFYDECKR RYNIKLWKTF TDCFNCLPIA
AIIDEKIFTM HGGLSPDLNS MEQIRRVMRP TDIPDCGLLC DLLWSDPDKD ITGWSENDRG
VSFTFGPDVV SRFLQKHDMD LICRAHQVVE DGYEFFSKRQ LVTLFSAPNY CGEFDNAGAM
MSVDESLLCS FQPPPPHQKP ENVLKRAHEL IGVNQTPAAL TLLHEHITSK RSRNVPIVSL
EPVMLLLVEL SVEQKKGKLA KDALYQYKNI SQNTNVGTIE LVLKKFIELA AEKVTAAQAK
ADEVQSTIDA STSTTNVEDL EASETPESIL LATVSGEQSR DRTDRAIVTP WLKFLWEAYR
TVLDILRNNA RLEILYQSTA MQAFDFCLKY ARKTEFRRLC ELLRNHVQTA AKYSSQMHAI
NLSDPDTLQR HLETRFQQLN VAVELELWQE AFRSVEDIHT LLNLSKRPPK NIMMANYYEK
LTRIFLVGEN YLFHAAAWSR YYTLLRQSAA LVASGQGKKA DNPPATDADL QKAASFVLLS
ALAIPVISTT RSRGAMVDFD ESKKNKNARL THLLGMAQAP TRAALFRDAL AKSLLKRARP
EIRDLYNILE VDFHPLSICQ KISPILTKIG DDAEMEKYVL PLQQVILTRL FQQLSQVYET
VDLSFVEQLA KFPEPFQVTR GTIEKFIMNG NKKGDLAIRM DHATGVLSFD NDVFSSAKAA
HSASGAGSAE ADGSSVQRLQ STPSEIVRSQ LTRLTKSLYT TCFYIDPEFN KSRVDAREAA
LARAKAGAEK EHRELLARKD VIQKRKEEAS EIQARKEREN ARQKRLREQI LQEQEDKRLA
AEQKEREERR LKAERDRVRK DELKKQIADL KISPKDMDLD LEDLDNLDPN TIRAMKVAQL
EREKNDVSEK LRIVWKRVDH LERAFRKEEV KKLGADYEEQ IQRDRAAYEK TKAQTLKDAE
IKHKESVELK HRLTRLMPHF ESFRENLHSR RGEEFEKRRR DAERELEKQI ATRKKEYRDR
KLREKREREE KERALREAEE RAAKEKEEQE ARAEAKRAEM QRLKEQRDQE RQESLEKAAM
QARREEEALA RRKAEKEKER ALPPMRSAAE PSSEGRRPLN LPGAGKWREK EAARGAAGAS
DNAPPAPRQS APMERTDSSD RAGGPPRLSL AGSGGKPSWR EREAARAAAG GAENSAPPQR
SERLERPERT ASGGAPMGRT ASNRDDQGRN ASPAPATEQL KASGAPGKWV PRHLRKE
//
