ID F4X232_ACREC Unreviewed; 1402 AA.
AC F4X232;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=General transcription factor IIF subunit 1 {ECO:0000256|ARBA:ARBA00020812};
DE EC=1.5.1.8 {ECO:0000256|ARBA:ARBA00012846};
DE EC=1.5.1.9 {ECO:0000256|ARBA:ARBA00012849};
DE AltName: Full=Transcription initiation factor IIF subunit alpha {ECO:0000256|ARBA:ARBA00031523};
DE Flags: Fragment;
GN ORFNames=G5I_12353 {ECO:0000313|EMBL:EGI59448.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI59448.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II and helps to recruit it to the initiation complex
CC in collaboration with TFIIB. It promotes transcription elongation.
CC {ECO:0000256|ARBA:ARBA00025232}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR EMBL; GL888565; EGI59448.1; -; Genomic_DNA.
DR STRING; 103372.F4X232; -.
DR EnsemblMetazoa; XM_011065767.1; XP_011064069.1; LOC105151833.
DR EnsemblMetazoa; XM_011065771.1; XP_011064073.1; LOC105151834.
DR eggNOG; KOG0172; Eukaryota.
DR eggNOG; KOG2393; Eukaryota.
DR InParanoid; F4X232; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd12189; LKR_SDH_like; 1.
DR CDD; cd00240; TFIIFa; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF50916; Rap30/74 interaction domains; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 499..629
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 669..872
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 181..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI59448.1"
SQ SEQUENCE 1402 AA; 157326 MW; C239DCE21846EDDC CRC64;
VAPSVQEFSI RVPKNSKKKH NVMRFNATLN VDFSKWSQVK MERENNMKEY KGIEEEMPKF
GAGSEFGRDA REEARRKKYG ITSRKYKPED QPWILKSGGK TGKKFKGIRE GGISENAAYY
VFTHAADGAI EAFPLHEWYN FQPIQRYKSL SAEEAEQEFS RRNKVINYFT LMLRKRLRND
EDGGDEEELA EGGKGKRPSK KEKELQISEM EEWENDESGS NEDEKKGSED EDDGKKKKKD
KIQLEKKKKK KNVSDDEAFE ESDDGDEEGR ECDYISDSSV SESESEPQKE VKSVAEEDAL
RKLLVSDEDE DEEEQTDKKD GEIDKDEDEE GKEKDDKDKD KLGKEMDKRK DKKKKKKAKK
KDQKKSASGK DSSSDFSSDS ESDSDTTLKE KDNKKPNSAH SSRSATPTPS ASGVSDSFKR
KQSGSPDLSQ AKKLKLDNFN LVPVTSYIPG TSESGITEDA VRRYLMRKPM TTTELLQKFK
SKKTGLTSEQ LNLKGKIIAI RREDQSVWER RAPLAPANVR RLVRSGVKVI VQPSDRRAYP
AQVYQAAGAL LQEDISSASV IFGVKQVPVD QLIPNKTYCF FSHTIKAQES NMPLLDAILE
KNIRLLDYEK LTDANGQRVV AFGKYAGVAG MVNILHGLGL RLLALGHHTP FMHIGPAHNY
RDSAMARQAI RGAGYEIALG AMPKSIGPLT FVFTGSGNVS QGGQEVFQEL PHEYVPPEML
RKVAEHGDTT KIYGCEVRRR HHLKRKEGDG FDPEEYDQHP ELYISTFSKK IAPYASVIIN
GIYWAVDSPK LLTIPDAKYL LRPANTPWLP ISVGAPALPH RMLGICDISA DPGGSIEFMN
ECTTIDTPFC LYDADRNKDT KSFKGPGVLV CSIDNMPTQL PKEATDFFGN LLYPYALDII
QSDAKKPLNE HNFSPAVHDA IIVSNGKLTP NFEYIQELRQ MNQRSRHKAD NREQQSKTVV
VLGAGYVSAP LVEYLHRDKN IRLIVASQLK DEADALANRF PGVEPVFLNV LDRPDTLHDV
IKSANVVVSL LPYSLHHVIA KACIETKNHL VTASYMNNDV KALHEEAQEA GITVLNEIGL
DPGIDHLLAI ECFDDVRQAG GKIESFVSWC GGLPAPECSS NPLRYKFSWS PRGVLLNTLS
PAKYLHEGQE VEIAGGGDLM STVQDLDFLP GFALEGYPNR DSTTYRDYYG LQNANTVLRG
TLRFKGFSDT ILGLQLLGLI DPNPHPILHP NGPDITWRVL ACNLLGLAND NIFYGNLKQK
LAERMNSWER VKAIEELGLL EEDLVLKLNT PLDTLTHYLS KKLSFEKNER DLVILRHNVG
ILWPDNRRES RGINLVLYGD ASGHSAMART VGYPAAIAVK MILDGEIQQR GMVLPFTPDI
YRPILNRLRT EGVQSFETSK WL
//
