ID A0A445G5T3_GLYSO Unreviewed; 1344 AA.
AC A0A445G5T3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN ORFNames=D0Y65_045610 {ECO:0000313|EMBL:RZB56541.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB56541.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB56541.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB56541.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF2 family.
CC {ECO:0000256|ARBA:ARBA00010937}.
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:RZB56541.1}.
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DR EMBL; QZWG01000017; RZB56541.1; -; Genomic_DNA.
DR Proteomes; UP000289340; Chromosome 17.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR15137:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:RZB56541.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000313|EMBL:RZB56541.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 248..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 151505 MW; 49D91706654BC3BC CRC64;
MAKPRKPKNN EDPKPENSGA VVHHQKLCLS IDIDKRQVHG YTELEIAVPE IGIVGLHAEN
LGIESVCVDG EPTEFEYYPH HQQQGEDEKR FSSVCSPSSA ADAAVSVYMS ALEKELVPNL
LINCCKPSKA ESEQQQEQQP TSENGFHSSA EPKQNVRTVR IDYWIEKAET GIHFRNNLLH
TDNQIRRARC WFPCIDDNSQ RCCYDLEFTV AYNLVAVSTG SLLYQVLSKD NPPQKTYVYK
LDVPVAASCY KDYLSVDFPF DSYTQVFIEP EMAVSSLSLG ASMSVFSSQV LFDEKVIDQT
IDTRVKLAYA LARQWFGVYI TPEAPNDEWL LDGLAGFLTD FFIKKHLGNN EARYRRYKAN
CAVCKVDNGG ATALSCSASC KDLYGTQCIG LYGKIRSWKS VAALQMLEKQ MGPESFRRIL
QTIVSRAQDK TRSIKTLSTK EFRHFANKVG NLERPFLKDF FPRWVGSCGC PVLRMGFSYN
KRKNMVELAV LRGCTALQTS NTSILDINPD TETRDGDTGW PGMMSIRVYE LDGMYDHPIL
PMAGDAWQLL EIQCHSKLAA RRFQKPKKGL KLDGSDDNGD VPSMDMRSNT ESPLLWIRAD
PDMEYLAEVH FNQPVQMWIN QLEKDKDVIA QAQAIAALEA SPQLSFSIVN ALNNFLSDSK
AFWRVRIEAA FALANSASEE TDFSGLLHLM KFYKSRRFDT DIGLPKPNDF HDFAEYFVLE
AIPHAVAMVR AADKKSPREA IEFVLQLLKY NDNNGNPYSD VFWLAALVQS VGELEFGQQS
ILLLSSLLKR IDRLLQFDSL MPSYNGILTI SCIRTLTQIA LKLSGFIPLD RVYGLVKPFR
DIKALWQVRI EASRALLDLE FHCKGMDSAL LLFIKYIEEE HSLRGQLKLA THVMRLCQMR
DGLNSNDEIT SQTLVSMLNL LEGRIAFNNA FLRHYLFCIL QILARRHPTL HGIPRENRML
HMSLTEASNY QKNMLALDSE SKPLDLPSSI DDLTQNLGPT MEGLRDALDE APKDQPCEAP
TQVHLEALKE ASLEKPKEVF TEFPQEAPIE APNEISKEAD TVSNSHERKR PIKIKVKQSS
ATSRADTDNQ VVERSLGGRN EMDHGASSSV SVDAPQRNFA ETVSISNHNI DEVNSWHDRG
SRMTASIGSA KFLSDGDELV KELQCTADSS IVYSQPQPED PSSSSIIQDN NIDADARRYA
SLQTLSVARF DPDGEPLGKE ISARGKEKHK SKEKKRKRES NKGHHDDPEY LERKRLKKEK
KRREKELAKL QSDEAKRSSI DMSSKKEEPV VDVVARQVTS VEPTGYDSKL EIKKIDTTKP
EPSEGTSGAP KIRIKIKNRM LSKP
//
