ID F2RWK4_TRIT1 Unreviewed; 1399 AA.
AC F2RWK4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Prion-inhibition and propagation HeLo domain-containing protein {ECO:0000259|Pfam:PF14479};
GN ORFNames=TESG_03146 {ECO:0000313|EMBL:EGD95678.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGD95678.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD95678.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG698489; EGD95678.1; -; Genomic_DNA.
DR HOGENOM; CLU_000288_34_8_1; -.
DR OrthoDB; 2479680at2759; -.
DR Proteomes; UP000009172; Unassembled WGS sequence.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.1020; Prion-inhibition and propagation, HeLo domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR029498; HeLo_dom.
DR InterPro; IPR038305; HeLo_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF14479; HeLo; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 16.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 8.
DR PROSITE; PS50088; ANK_REPEAT; 9.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 7..160
FT /note="Prion-inhibition and propagation HeLo"
FT /evidence="ECO:0000259|Pfam:PF14479"
FT REPEAT 751..783
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 817..849
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 850..882
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 883..915
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 916..948
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1011..1043
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1049..1081
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1183..1205
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1250..1282
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1399 AA; 154412 MW; E49902D587C04F9E CRC64;
MEVASLVLGV AGLFSVCMDV LDRVSNYREF STQSRQTVVL FEANKVRLKE WAAYAGIENG
VLKDSHHVRL DEPGILSAIK LVLEEISTLF DSIERSQSRL RIPQVVVSPA GSGGGASKNG
SKPSIRGGIS WSSRGKESFT SQVTIFGGFV DTLHDLLPKE KDGSGSLVKD FKALLIETRK
NTLIQTQKRV DEWLDAPETE QQYETHLSAC LDGTCNWITA ELAYKTWESD YFPGETAKFL
WICGPAGSGK SVLCAKIIQR FTEKSNHPLA YFFSTGHVQA GGHPDGAVRS WISQATRHDE
RNLELVQQAM DHAEAGRRAS QAEVWKLFKA IASDTTPYTF VLDGLDEYEI HYDERAHLLR
GLKEQAKGVK CRVLIVSLDE VDLNQELSPS PGNKEGTTML ECQISKSKTK SDIQLYSESV
VNKKLGKKGA SLRRELATQM AEKCGGMFLW IKMQQDQLRG GKNDKQLRNI VSTMPVGLHQ
IYERNWANIQ RRPANERRRA MSILRWATFA YRPLKLSELV QALAICDGDE EEIEEQEEGN
CENDLNDDEP PEFPVDELPE EIDEEYVNGE IKELCGSLIE VRIEVPDYMM RWNIDTPQGY
GTIHLVHASV KEYLLLKFAN SRNISSPSNP SPTASQAVQH SILAKTCLRY LTYPEVWDGG
VLPTFDVDDG SFLNYAATSF DTHALAAGKN SQLARQISHF FHKSPNFIRW KHHVGGVGAG
PLYHSCRLRL LDVARISLKE HGEDPDALAG RFGTALQVAC FGGEMPIVEL LVESGADVNL
EGGEYGSAVN AAIAIGDNYI ISYLINKGAK LDTKNKEGRT TIHHSAKNGN IKLLERLISN
DADIAIADNE GVTPLHLAAS SGNLGTVKFL LEKGADIEAV TSTGRTPLCY ACQAGNTDMV
KLLVREGADI HHAPSSGNTP VYEASCQGRT ETLQYLINQG AVVTAESKAL KDAASEGYIA
VVKLLVKAGV SLEDVVGDEA LYNASLNGRT WVIKFLLLEG VKAENVRDPA MNCTPLFWAV
LGGHTNIVKL LLWKGASPNI HPSMTKDVAN ETMLVNAIRR GLTEISKALL RKGANVDPEH
NFGISPLCEA IVRDQVEIVH MLRLRGADPT KRGNLRYTPL LQAAIRGNEI MFMHLVRGLA
GTTNASVPKK YGTFLNAAAY GGSLSLVREL AKVCGPTQYK DSEGRNPAHF AARGGHADVL
KFFLDDDGID PQSLDIAGRG IVHHAACGGS VETLRVALEA QPPDVKFTEN TWSPLHWACK
RGSVEIVNLL LEYGVKESTV TTTDEPAAEW TPFRVAVYHQ NKSLVRDWSE TKYKLDDTIV
LQGYHSISLA GCSWCLHELY GPRYYRTSRS GLVLCFMCKH TADTVYPDSK WKSEYCEELW
TTDLNEGPKW EAPEIGGFY
//