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Database: UniProt
Entry: A0A0V0UWY3_9BILA
LinkDB: A0A0V0UWY3_9BILA
Original site: A0A0V0UWY3_9BILA 
ID   A0A0V0UWY3_9BILA        Unreviewed;       928 AA.
AC   A0A0V0UWY3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Transcription initiation factor TFIID subunit 5 {ECO:0000256|ARBA:ARBA00044130};
GN   ORFNames=T09_12715 {ECO:0000313|EMBL:KRX55812.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX55812.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX55812.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX55812.1};
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   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- SIMILARITY: Belongs to the PIGX family.
CC       {ECO:0000256|ARBA:ARBA00010345}.
CC   -!- SIMILARITY: Belongs to the WD repeat TAF5 family.
CC       {ECO:0000256|ARBA:ARBA00009435}.
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:KRX55812.1}.
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DR   EMBL; JYDN01000136; KRX55812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UWY3; -.
DR   STRING; 181606.A0A0V0UWY3; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.25.40.500; TFIID subunit TAF5, NTD2 domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013233; PIG-X/PBN1.
DR   InterPro; IPR007582; TFIID_NTD2.
DR   InterPro; IPR037264; TFIID_NTD2_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19879:SF1; CANNONBALL-RELATED; 1.
DR   PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR   Pfam; PF08320; PIG-X; 1.
DR   Pfam; PF04494; TFIID_NTD2; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF160897; Taf5 N-terminal domain-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Initiation factor {ECO:0000313|EMBL:KRX55812.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000313|EMBL:KRX55812.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          346..453
FT                   /note="TFIID subunit TAF5 NTD2"
FT                   /evidence="ECO:0000259|Pfam:PF04494"
FT   REPEAT          675..716
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          759..800
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          801..842
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          843..884
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          534..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   928 AA;  106063 MW;  51A4FF7253FC6520 CRC64;
     MCILKITYIL LFCGFFTYLY SNDLSLKKDF KITGDGFHRQ LSNFIYLSSM NRLVNCSVVY
     RVTVPSGAYL DVDQMPASIR NIFYSYKPFF VEAPAWTSVD QTVLIESSKR MYNAFIFEDV
     IEFPIHFRYQ KPTKGGLIVK VRFYAPDVLL RCLDPKFLDL LNFTGGADDS RLVEAPCNFY
     YNYTSTLLCL YLHVKESSVS YADIDIPTPD ISYKVPVTIG LILCIIYSFC TTVYTLLACC
     SETTGDFRDV IFRHSTVLLH QNDFEKKILI SMAEMSDMQI DVDEYSRINE KAKCTFRLLD
     LLGASETRSA FINGLQARSA EITDARDYFK PPSQFERDEF AKRKFESAVK EYSTLISILK
     QSVSDRCQPE LSVFNFTVYA AIFADFCYND QFDLARDFLE KFLPIQECYY ESIIEEFSLV
     LDEQDVQFCL PLRELKSNRI VVRLSRESIS EFRELIKSLP LISDIVEARF ELDTSDEPAR
     SYETVERYRG YLLGEAPLKM MKTKVYSGIF KDQALPILAD DSTRFFDIDG DLEKPKKKKS
     KSKDSTTTRK QKADPNAPAW GRIPFGQLSD TWKLKRHQML SEINRKPKAN VELRPTAIFY
     AVENSDEAID AITTSEDCKL LFLGYSNSSI TMRSLNEEPL PTLKRAEELE SLNIDSDDIY
     TEMLEANPTE VEYVLTGHTG EIYSLSYHEE KHMLLSCSQD KSIRLWNLLT RDNLVAYHYD
     VCEPTDVQFS TFGSYFVSGY FDGAVCLWAL DRPSPLRVML GHYDLVGRVR FHPNCNYVAS
     CSEDRAVRIW DLLNGQCVRL FTGHKASVQA LEFSYDGRWL ASGGEDGRVL VWDIGSGKMM
     HDFINHRGIV YSLAFTRDSR VLASGGTDRN IVIKSLVSQN SSTVVNDTNL LSSTAHSREH
     TFGVEAASAQ YLRFSLRNVL FAFGGVGQ
//
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