ID A0A1E4RIP7_9ASCO Unreviewed; 779 AA.
AC A0A1E4RIP7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-OCT-2025, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ODV66975.1};
GN ORFNames=HYPBUDRAFT_161864 {ECO:0000313|EMBL:ODV66975.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV66975.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; KV454541; ODV66975.1; -; Genomic_DNA.
DR RefSeq; XP_020076042.1; XM_020222543.1.
DR AlphaFoldDB; A0A1E4RIP7; -.
DR STRING; 984485.A0A1E4RIP7; -.
DR GeneID; 30997092; -.
DR OrthoDB; 5954824at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:2000221; P:negative regulation of pseudohyphal growth; IEA:UniProtKB-ARBA.
DR CDD; cd00059; FH_FOX; 1.
DR CDD; cd22701; FHA_FKH1-like; 1.
DR FunFam; 1.10.10.10:FF:000030; Forkhead box protein K2; 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; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR018122; TF_fork_head_CS_1.
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; PTHR45881; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR45881:SF1; FORK HEAD PROTEIN HOMOLOG 2; 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; PS00657; FORK_HEAD_1; 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:UP000095085};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 76..139
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 246..344
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 246..344
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..526
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..643
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..742
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 85692 MW; F66436EA453FFDF5 CRC64;
MSGTTTPRKR NLEDDLPSFD DPADLVNAVI STLQQPEDRT NVANNYANDK NHATEIQAYA
KIAGQDWTFY VKSLAVSIGR NTDNPGAANN SNTPLIDIDL GPAKVVSRQH ATITYNIDLS
CWELKVLGRN GAKIDGQKMP VGIQHATPLH LGAILDIGGT QMIFILPDSP PDILPKMLST
CLSKYKSNMN KVRKSSSSSY SHSGPVKSFQ MFDKAQLTHS PSSVSASSLQ NNLDQDLSKV
EAKDIKPPYS YATMITQAIL SNDDGVMSLS DIYNWISDHY AYYKYSKTGW QNSIRHNLSL
NKAFEKVPRR PNEPGKGMKW QISESYKQDF LNKIQNGSLL KTRRGSSVSR QLQLHLATHQ
QLPDTQKYFD KNEKANSQPP QSTHQQSQPP QLHQRSDSYD YRFSHSRNNS IPNLGQPMQY
PGIPNNPIQS NPLSYLNQPN GGFMGIPPNA SRAYSPYQPV AAPAHFMYGT SMLNQSAPPP
PIQQQLQPQH NNANIYLAQQ QQHQQPQPQP QQPQPQPSQQ VPSAPQNSLN KPKSNEDNQA
SDQKTKSELS SPMRQESNLN STTPKLPKVT SGGHLFNLPP PSSNSHNVGS SAPQAHHSRL
HSYNNNTNGG QDTGNSFGNS TNNPNSSESN QNNTTGQTNN TSEFGMGFTS PKKIAPLEAF
TPERGSKSNG ANKLGVPNGS NTNQSSPAFW NFVQFSTPNA QTPLRKNSDE LNSQGSPTLS
RKNLSNGLKN EDDLNNNDEE NENGVSTNDD GSPSEKADVK IELDSKSDLN SRKDEPVST
//
