ID A0A177D5R8_ALTAL Unreviewed; 645 AA.
AC A0A177D5R8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Transcription initiation factor TFIID subunit 12 domain-containing protein {ECO:0000259|Pfam:PF03847};
GN ORFNames=CC77DRAFT_947854 {ECO:0000313|EMBL:OAG14848.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14848.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14848.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14848.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF12 family.
CC {ECO:0000256|ARBA:ARBA00007530}.
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DR EMBL; KV441497; OAG14848.1; -; Genomic_DNA.
DR RefSeq; XP_018380269.1; XM_018535168.1.
DR AlphaFoldDB; A0A177D5R8; -.
DR STRING; 5599.A0A177D5R8; -.
DR GeneID; 29120762; -.
DR KEGG; aalt:CC77DRAFT_947854; -.
DR VEuPathDB; FungiDB:CC77DRAFT_947854; -.
DR OMA; INMAIPK; -.
DR OrthoDB; 22237at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 12; 1.
DR PANTHER; PTHR12264:SF21; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 12; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 535..604
FT /note="Transcription initiation factor TFIID subunit 12"
FT /evidence="ECO:0000259|Pfam:PF03847"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 71959 MW; AE9813CFC321A925 CRC64;
MSDSQPQQAS GGQQGQQLLR PDDILKLQCL PEDEKQKYRL IMQNFWTIFN NNPQGSQENT
NARQKLTEWS QKFIGRERQY RAKMKQQQQQ GNQNQGQAGQ SSAAGQQNAN AVKQEGGQAQ
PQGSGAPANQ QSQGQQQPNQ GQNPGRGQVD PAIVKHVHDF PMQGPTNGPT PGTPEYENKL
KEYRTGYLNM LAKQATLTEQ RRRIIQELTE RQNNGQELPQ ERLLMKNNIE KEAAKIKAQI
DKFRAMQKQW KEEREQNSQG QAQAQGQNPA QSPPQQQPQP PQRQPSQPNM PAQPQVKEEP
QIKIEGGQAP QPQPQTQSQP QPQFNMQANQ GNLQQGPPQQ QQMQHNQQLP QQQQMQQQQQ
QQARPPPAPH SQTMPPNQMP QFSQQGQQQQ NFHQQQQQQQ RPQINPMQAN AHQQSNSPHP
QSAASNAPGP PVPLSHQAAV SAANRSYTDP QRTNTPMQQG GQGGNFGSRE REQLNNPKMP
IPRHLNVTSP QAVHMGQARP TMSGPTNGAP GPMGQPVIPR PPPFQLEGEG DRVLSKRKLD
ELVRQVTGGS EEALTPEVEE AVLQLADDFV DNVISNACKL SKLRDSPQLD IRDIQVILER
NYNIRIPGYA SDEVRTVRKI VPAQGWANKM SAVNAAKVMG GKADF
//