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
//