ID A0A3Q2ZU73_KRYMA Unreviewed; 1037 AA.
AC A0A3Q2ZU73;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transcription initiation factor TFIID subunit 4-like {ECO:0000313|Ensembl:ENSKMAP00000001839.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000001839.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000001839.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF4 family.
CC {ECO:0000256|ARBA:ARBA00006178}.
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DR RefSeq; XP_017284141.1; XM_017428652.1.
DR AlphaFoldDB; A0A3Q2ZU73; -.
DR STRING; 37003.ENSKMAP00000001839; -.
DR Ensembl; ENSKMAT00000001885.1; ENSKMAP00000001839.1; ENSKMAG00000001447.1.
DR GeneID; 108243306; -.
DR GeneTree; ENSGT00390000011620; -.
DR OMA; HQEMNSK; -.
DR OrthoDB; 2910924at2759; -.
DR Proteomes; UP000264800; Unplaced.
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 GO; GO:0006366; P:transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd08045; TAF4; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.20.120.1110; TAFH/NHR1 domain; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR PANTHER; PTHR15138:SF22; TAFH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR15138; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 4; 1.
DR Pfam; PF05236; TAF4; 1.
DR Pfam; PF07531; TAFH; 1.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF158553; TAFH domain-like; 1.
DR PROSITE; PS51119; TAFH; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 576..673
FT /note="TAFH"
FT /evidence="ECO:0000259|PROSITE:PS51119"
FT REGION 27..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1037 AA; 108027 MW; B510D6967BCA1F50 CRC64;
MAGASDPLED MLFSEVDEKA VSDLVGSLES QLTGQSSSAG KTDENGGAGS VAPANHHLGK
TLPAPVSTTT LEQQQQGRRN KPEMRQEINS KDASPDKTVT SPSLGSTSAF GEPPTTSAAC
VNTTSSGPQS HGASITTLAA SGGSTLAPPQ DSISTASSRS SKASPGAGDT PAEAGTPRKR
AATPRRSASA RIKSLNGAAV TTRRNSGAAA AENASSSVAT TPPNSTRPLT SSINTSTFTL
SNASLPVGQS AIALDRGTPT IALRRLPSHI VASIAQNGNG TSVSALVVQQ GARLGPVTSS
ASPEDHSKPA TDSGASNVDD CQSKIVISSQ SSSVSSVINT VSSTSSAVTA APTTTAAPTT
TTSSPPLSSA TTTTAVCGTG TATSTACVTA QTTSVTATTT TISMVRPTAP SPTPAVATSA
QTQPRPGLAA PQRIVAPQLI VRPSQQQATI QLPPGFTIPP GMVLVRTELG QFVMVPQQAL
AQVQAQAQAQ AQAQAQAQAQ NNISPRPATP TTGTSFRVTT PQKAPVAPAV AVTAPQQTPV
VMAPQGPAQS TSQPVQPAPT SVTAAPGAPV VSQEMQENVK KCKNFLATLI KLASHNSPSP
ETSKNVKALV QDLLDAKIEP EEFTSRLQTE LKSSPQPYLV PFLKKSLPAL RLSLLNSQQS
LTQPLQQGVK PAASGTPPAI VAGPAVRIRH PNSVSTTVSA TALPAGTLGH TAAMGVKTGG
VVGGQVRMPM VITQSIRPQG TIGKGAIIQT GKSPMGLPVQ ISGNQKNKLN DPGGGSFRDD
DDINDVASMA GVNLNEESAR ILATNSELVG TQIRSCKDEA FLHPGLLHRR ILETAKKFGV
TEVSMEAVTF ISHATQSRLR TVVEKVSVIA QHRLDSCKDD ECYEQTGDVR SQLRFFEQLE
RIEKQRKDEQ EREILLKAAK SRSRQEDPEQ ARLKQKAKEM QQQEEAQMRQ RDANLTALAF
IGPRKKRKLD SPGTTPSGSE VSGSMAGSPA GSSAPSTSSR QYTRQRITRV NLRDLIFYME
QERETAHSLL LYRALLK
//
