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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//