ID A0A059JIL9_TRIIM Unreviewed; 1129 AA.
AC A0A059JIL9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=CCAAT-binding factor domain-containing protein {ECO:0000259|Pfam:PF03914};
GN ORFNames=H109_00510 {ECO:0000313|EMBL:KDB27716.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB27716.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB27716.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB27716.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CBF/MAK21 family.
CC {ECO:0000256|ARBA:ARBA00007797}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDB27716.1}.
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DR EMBL; AOKY01000038; KDB27716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059JIL9; -.
DR STRING; 1215338.A0A059JIL9; -.
DR HOGENOM; CLU_003417_0_0_1; -.
DR OMA; EIWCNDE; -.
DR Proteomes; UP000024533; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005612; CCAAT-binding_factor.
DR InterPro; IPR040155; CEBPZ/Mak21-like.
DR PANTHER; PTHR12048; CCAAT-BINDING FACTOR-RELATED; 1.
DR PANTHER; PTHR12048:SF0; CCAAT_ENHANCER-BINDING PROTEIN ZETA; 1.
DR Pfam; PF03914; CBF; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000024533}.
FT DOMAIN 672..847
FT /note="CCAAT-binding factor"
FT /evidence="ECO:0000259|Pfam:PF03914"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..801
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1043
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1081
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 127082 MW; 259169C4DFD464EE CRC64;
MAKGKGKEDK SLKARDGAAT EKKRPSNDAD ATPSFSDATV ANLTKRIEQK LKGDEGGNGG
LSKAEKKQKS EKNEKRKERN QAIETKPTEK PVKKRELLAD VKPTDKAGKK RDRSGKIIKS
DISENPYSTA ERQCDGGKSL EEEVYAIGGT KEDLDLVAGV ESDSEMEDKE VSSGDLEKLR
RDLGRLINGG NELPEVPELP VQETKPIKTK QDRKQEGKQS EENRTEKPAQ EKKSKGNNAL
EQRTESKKPQ KNDSLPSALT QDSKIPKKGL SSSNLVIPER SDWYATQLPD ISYDSSRHVN
VSRPVLERMR EYAMTLLEAE NKAYTSNRDS KSSSYKFYST IVSSGTLSDK ISALTLSAQE
SPLHNTQALE NLVGLAKKRS RAQAVEVLRS LKDLFAQGTL LPSDRRLKHF VNQPALAAAL
SEAGGHWDIG DKLPNQIEKS HLIMWAFEDF LKDQYFEVLK VLEVWCNDEI EFSRSRALSY
VYELLKEKPE QESNLLRLLV NKLGDPSKKI ASRASYLLLQ LEQAHPLMKG TIVSSIESES
LFRPGQSQHA KYYGVITLNQ TILSKSDDKV AAQLLDIYFP LFVALLKPKT DVHAQKKLKK
KGKHPKKGKK GKEDNDDAKG EAQEDELREK LISAVLVGVN RAYPFTTSSY ELLSKHLDTL
FRITNSSNFN TSIQALMLIQ QLSSSHAVSA DRFYKTLYES LLDPRVATSS KQSMYLNLLY
KALNTDINIK RIKAFIKRLV QILGVHNPSF SCGVLYLIQK LETTFPSLTA MVDQPEDAED
DDEEEVFRDV PDEEEDEMVD KEEPEKQPSV TRYDPRKRDP EQSNADRSCL WELLPYLSHY
HPSVAVSAKQ LLLHEKMSGK PDLTIHTLTH FLDRFVYKSP KAAPSLRGSS IMQPLAGGDS
SGLLVTSGRN TTQQPVNSES FWRKRSDEVS AEDVFFHDYF NRLGKDKLRQ KSKKKSAKDD
EEGESDEESE VWKALVQSQP ELDGEGVSDD DMDMDGFDSA MEDSDRDDLE GMDEDIDGED
REIDDDVIIN DESSEEEKDD EEAPSEAGMD KSIDIDEDVF NFDQSDEEAF LDSDQELPSD
LDDEVAEAKD TKKSDQPKRE KRRKLKHLPT FASVENYAAL LGKDDDEDF
//
