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Database: UniProt
Entry: M2RKF9_CERS8
LinkDB: M2RKF9_CERS8
Original site: M2RKF9_CERS8 
ID   M2RKF9_CERS8            Unreviewed;      1092 AA.
AC   M2RKF9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Transcription factor BYE1 {ECO:0000256|ARBA:ARBA00021616};
DE   Flags: Fragment;
GN   ORFNames=CERSUDRAFT_104220 {ECO:0000313|EMBL:EMD38932.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38932.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD38932.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD38932.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC   -!- FUNCTION: Negative regulator of transcription elongation.
CC       {ECO:0000256|ARBA:ARBA00002311}.
CC   -!- SIMILARITY: Belongs to the BYE1 family.
CC       {ECO:0000256|ARBA:ARBA00011050}.
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DR   EMBL; KB445794; EMD38932.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2RKF9; -.
DR   STRING; 914234.M2RKF9; -.
DR   HOGENOM; CLU_011239_0_0_1; -.
DR   OrthoDB; 5491784at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd21538; SPOC_TFIIS; 1.
DR   Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR036575; TFIIS_cen_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11477:SF20; PROTEIN PARTNER OF SNF, ISOFORM B; 1.
DR   PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          44..94
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          245..397
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000259|PROSITE:PS51321"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..487
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1007
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMD38932.1"
SQ   SEQUENCE   1092 AA;  118402 MW;  9440C9DA3A4ED3D8 CRC64;
     MTSRPTGRTR QSRASDAASP HNKENATING EKTRGKAKPR VEGKVYCSCR KPDDGTPMIL
     CAHCKEWYHF QCLKLSERDA EDIEVYICPP CHEKTGLRSV MEWEGPEAIE EAKQSANRAT
     PPNADDIKKE EDANTKMEDA PELPSESEAE SSADDYVAEK SPSHSKRRAR PIPSSDSESE
     SIASAKASRT TKRLRRGSAA KKEPARRTVS TSPGPTTQTK RRQSTASQSE TKRMRSGSTS
     SDDPARKYCL NKLQEMFCQI FVRYPFFKDD VIAVGDLQPD KKQEELSDEE KEALEHRAKR
     FASDLEQCMY EIYSEPDKNG KHGVAGKYKE RFRMLTFNLN QSDRAVLHMR IASGQIPPKE
     LSTMSSTDLA SEEAKQSIKQ AEQEALQQTI LKKQALPRAK ITHKGLQDIE DVNGGSPRAA
     ERAREDEEEE RIERERLARL RVQTQRSNSG QGSVPPDSPV VPNTPQTPLT PLTPHTPRWG
     APPPVPGALH GPQPSELMPP PSVVVPRPPV APLFVPSGSE FVGAPGESEL NLADFINIDD
     EPTSDVTLST AEPPLTPTVT AAPVITPIST AQATPTHAAP PTIGISPFAQ RSADERRPSF
     DLNALWSPKA ADSNYEHQSG PQEAGHAPMY EEPKEIGESN VISEEAEDQD FDMFLGNDEM
     ERATDPSNED AMAQDTPFDV QPTVWNGTLN MPLDSTLAQE VSLVARQGGG RPLGNDSPLW
     RALFPSPQLR IDGRVPVDKS AAYLTQTRLN PTKELIAVAF SPAPGTDVSG FQTLIDYLIT
     KGRHGLVFPW GNRPKENAPG RELYIVPLLS HEPLPEFMEL LDDLRLPKMR STHYLVGIWV
     LTKGKLTAPT TPPPPPAPVQ VPVPAPAPTT APTPTLTIPA FDPSQLQHLI PALTNAHAST
     SAAQMPPSAP APVLPAVMTA SNAALAAEVA SLTPEQIQAM LLALQNSGLS PPPPAQPASA
     PPPTSTSMTS IPLQPWTAPV AAYPPSYPPA NAYPSQPLPP PAPRQYPDMP YGGYDHGAPY
     PPGGGHYDGG GDRGYRGRGG GGAGGGRGRG RGRDRDRPRD TGWPKSRGRG RGGYASAPRG
     GGARWGENQQ WS
//
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