ID   FHL1_CANAL              Reviewed;        1152 AA.
AC   Q59ZC8; A0A1D8PHS0; Q59Z64;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Fork-head transcriptional regulator FHL1;
GN   Name=FHL1; OrderedLocusNames=CAALFM_C206830CA;
GN   ORFNames=CaO19.2236, CaO19.9778;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=12455696; DOI=10.1128/ec.1.5.787-798.2002;
RA   Bensen E.S., Filler S.G., Berman J.;
RT   "A forkhead transcription factor is important for true hyphal as well as
RT   yeast morphogenesis in Candida albicans.";
RL   Eukaryot. Cell 1:787-798(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=20231876; DOI=10.1371/journal.pbio.1000329;
RA   Lavoie H., Hogues H., Mallick J., Sellam A., Nantel A., Whiteway M.;
RT   "Evolutionary tinkering with conserved components of a transcriptional
RT   regulatory network.";
RL   PLoS Biol. 8:E1000329-E1000329(2010).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH IFH1 AND TBF1.
RX   PubMed=23625919; DOI=10.1074/jbc.m112.436683;
RA   Mallick J., Whiteway M.;
RT   "The evolutionary rewiring of the ribosomal protein transcription pathway
RT   modifies the interaction of transcription factor heteromer Ifh1-Fhl1
RT   (interacts with forkhead 1-forkhead-like 1) with the DNA-binding
RT   specificity element.";
RL   J. Biol. Chem. 288:17508-17519(2013).
CC   -!- FUNCTION: In complex with IFH1, acts as a transcriptional regulator of
CC       rRNA and ribosomal protein genes. The FHL1-IFH1 complex is targeted to
CC       the ribosomal protein genes by the DNA-binding factor TBF1.
CC       {ECO:0000269|PubMed:20231876, ECO:0000269|PubMed:23625919}.
CC   -!- SUBUNIT: Interacts with IFH1 and TBF1. {ECO:0000269|PubMed:23625919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; CP017624; AOW27684.1; -; Genomic_DNA.
DR   RefSeq; XP_714827.2; XM_709734.2.
DR   AlphaFoldDB; Q59ZC8; -.
DR   SMR; Q59ZC8; -.
DR   BioGRID; 1226587; 2.
DR   STRING; 237561.Q59ZC8; -.
DR   PRIDE; Q59ZC8; -.
DR   GeneID; 3643493; -.
DR   KEGG; cal:CAALFM_C206830CA; -.
DR   CGD; CAL0000186899; FHL1.
DR   VEuPathDB; FungiDB:C2_06830C_A; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_005476_0_0_1; -.
DR   OrthoDB; 1270467at2759; -.
DR   PRO; PR:Q59ZC8; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008796; F:bis(5'-nucleosyl)-tetraphosphatase activity; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0004780; F:sulfate adenylyltransferase (ADP) activity; IBA:GO_Central.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IEA:UniProt.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProt.
DR   GO; GO:0009164; P:nucleoside catabolic process; IBA:GO_Central.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProt.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1152
FT                   /note="Fork-head transcriptional regulator FHL1"
FT                   /id="PRO_0000426079"
FT   DOMAIN          171..229
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   DNA_BIND        659..756
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          55..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          449..537
FT                   /evidence="ECO:0000255"
FT   COILED          734..777
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        65..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1091
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  126115 MW;  5EDFBB9B834E3478 CRC64;
     MSHIDGDDHM TKDLIDSLES KDNDLSLVTS NTQIPDVEVA NLTHDADEIN QLFDTATNNV
     LPESNKKDKP IDTQDLHEDD PKAVPKTTSN GESTSNSNSV SPKLLPNDGK STPKIQKELR
     RKSTFVPVTS NSKSLEPSED DNNNNNNNSR ISAYARLDFE NFTFFVQTLQ VVLGRKSNDE
     TLQQNVDVHL SSKKAISRRH AKIFYNFGTQ RFEISILGRN GAFVDNVFVE KGLTIPLTDG
     NKIQIGDIPF KFVLPSNEPN EENNNQDSSE KQFNPSDAIN LRSNLYSKSS SPQSSPKRKP
     QPSKKVKKEP VSASNTSKDI KPTPPVPTTA ISPTASISTS TNAATAATAT TPATTTAARK
     NSINRRNSLL KIRRLSNARR KSLAANDEIN ELLKDLGVTS IDEINEEDSE LLDAQIQSLL
     DEDNENLGGI EDSLMKLAEF NESAIDDDDD DEEGNENSQA DLDRLEKTME HDAIDDEIKA
     IDSNLTLLDD EISKLTPLIN DTNQGLLEEK ETKKKQLEEE KRKKQLQQLQ HKNSLAKFPR
     RSAPLMGKPA SIQPPASSSI YSRINGLDKI GKTVSPRPPP PKLIAPVLRV TAEPSAIRSR
     PPLRAITVSD SSYIATFSYP KTIEEPSKYP KPKVKKEHHK KHSKKVYSLD EIPEPYRSKP
     NISFQIMITN VLKTEAARNG LIINEITEAI KEVYPYYKYC TDGWQFSINH CIKFTKIYKR
     LQKRGSEWLY AMDELYINER ENIRIKQREI AKAKAKAEAL RQEEIRQRQR LEAQKSLPHN
     IVGRNFASPY ANTRVPPNQY NQFSQSSSSS SSSATTTTNG QYGSTTMVGG TSPQAGSIRA
     QLAAVRGNGN TPATTSTTPS LPAMNDPKTK KSLEYLQKEL FTLYKARKLT YDTQTATSLI
     TKAVATTIAQ VNSIGAKAGA GDNALVFLVE RAPEKVSKIL DIALTKSIKE HEGIASKSPS
     QPATPGMRPE QLTTTSQSAA TPTTTPQISN LQSLPVKPPI STPLPQVPQQ QVSGVNIPGP
     IATPNIGVTS GVGNLGTTSI GTPTPTQIQS PATSVIPAMQ SPQKPVSTPI PTSVPVPLPV
     PSAPLARPPS FGKPPGAGSS LSRPKAFGKP PGAGSSLSRP PTFLSNKPSY KRELEDDEEE
     GEQATNKIAK TE