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Database: UniProt
Entry: I2H0Z7_TETBL
LinkDB: I2H0Z7_TETBL
Original site: I2H0Z7_TETBL 
ID   I2H0Z7_TETBL            Unreviewed;      1545 AA.
AC   I2H0Z7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Pre-rRNA-processing protein FHL1 {ECO:0008006|Google:ProtNLM};
GN   Name=TBLA0C02390 {ECO:0000313|EMBL:CCH60049.1};
GN   ORFNames=TBLA_0C02390 {ECO:0000313|EMBL:CCH60049.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60049.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH60049.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   EMBL; HE806318; CCH60049.1; -; Genomic_DNA.
DR   RefSeq; XP_004179568.1; XM_004179520.1.
DR   STRING; 1071380.I2H0Z7; -.
DR   GeneID; 14495029; -.
DR   KEGG; tbl:TBLA_0C02390; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_003924_1_0_1; -.
DR   InParanoid; I2H0Z7; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000002866; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00059; FH_FOX; 1.
DR   CDD; cd22701; FHA_FKH1-like; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR045178; Fhl1/FHA1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR   PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT   DOMAIN          730..787
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          952..1039
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        952..1039
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1300
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1335..1365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1429..1444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1445..1482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1545 AA;  171574 MW;  DFE5866841361E7C CRC64;
     MIMSTDQLIP ISDSNNALKT LPQQNLDGTN LPDPPSQQAI ELQENKHPNN NNDDDNDDTV
     IGKDLNEEEM DKETDAASYT NQHDDTPLIR RPLNTSTEEL IINHSTNNDD PISKTNNDNE
     TNENNLQSIH SDVNSNILEI DELPNELTLP TLDDDLEQKT DDKTNTDIPS DQELNISTDI
     MHKEESSTIP TDSAELTSNE LSTNVPDNLP SERPTQQQSE ILNKLPSEIS NKLPSEISTL
     SNTNLQNIKN SNDNSSDPEK FEIQTSLEQE KQTNSNKTTN NLSESINETI EIISNDSTTT
     DSGISYKGGS ELTHKDSGDS QEKIDLQKLE QNSPKTIIEL PKDLDAFPEN IDEISSKIEN
     LSEELGEEIE ENMDTIPKEL KISINEISKQ QGSKKDTSIK EDPPFRLTST DDSKHILNDS
     TKLKNNYQDS NSSNNEKNSS DDDTNKSSGI ANEDSDTDDE KDAIDAEVFS KLLDFEAEID
     PDELFSPNEL LPPTLSTTII DMDTSAKSPT NDSSSNISDK DSKKNDIPEL PTLEDEEELF
     DNLPLLSNNS SNKSNDISQR SSSNFNEKLT EPNKDLPNDE PSILSLKNEE DHDSKNEEHQ
     KQLDQHTPAF IIHEKNNLLY PSRKNSLTPV TLYGKYDSPS SRFQNKILKP NTISNIQTDK
     SGVKNNDQPV NNANSQSTLP TNPDNNQLNP KDLTNLLYNG AQRLSDESKI SAYARLDFQS
     FTFYVQTLHV ILGRRSENDF SHKVDVNLGP SKSISRRHAQ IFYNFGTGRY ELSVLGRNGV
     FINEQFVEKG HTVPLKHKTK IQIGEIPFQF VLPEQERDPE DEEDIKSSPA IPDMNALEID
     DEDKHLIGNG HDDSNTSLPD LNDNEFMPLD DDMDLDDKPL IQIKQSKISS SSISTTSTSK
     PQTLMKTTSV KTSPAKKKKI QIKKEPPKEK KPAREPKKVY SINEIPPEYR NKPLISYSVL
     LTTCIRKYAT PKGMSLSEIY NAIRETYPYY KYCRDGWQSS VRHNLSLNKS FRKVSKGGKG
     WLWGLDEDYI TERDRQKKVQ AETAANKAKA SQMKVKQQQK KVKKSVNLNP IKQPITPSYN
     ANNKRQTISQ TLAANRAATN NNKANKANDQ RRTMKYLQEQ LIILTRDRKG LQKATITDIL
     TQALAMTINQ VTKAAKSKGI SGNPLTALMD KNPQHLNLIL AAAVNAATVK VTKGKVKSLV
     DLSTVTLPTV VPGANSDTSS TRPTLTQTIT RKNPSDNSFD PTSLSRFFQP RQNSSNTNNS
     TPKITVQSMS KNSLPQKRTR DDSDNEEGDD DEEEDSSSDS SSNDSDSGSN SDSDIDSGSD
     NDTGSSEDSD DGSGSDNESI NSSGSDSGDS SDEESGSSSG TDNDSDDSDA GSDRDSDDES
     RQHNEYSSSK DKIQGDAHIV VDDANNNDIT NTKSDELLND RSGSEEKETH STGFSLSPPA
     FKSTEHKHSN SENDSEERTL QSADNKHDSE LEEKKELEVS YNDSLNKSHS QSPPIDHTDI
     DAISSLDNEL QNSEALHELQ SANPDIASGD IELSPLDGTL EHASQ
//
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