ID G2YSG6_BOTF4 Unreviewed; 789 AA.
AC G2YSG6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Similar to RNA recognition domain-containing protein {ECO:0000313|EMBL:CCD54564.1};
GN ORFNames=BofuT4_P126120.1 {ECO:0000313|EMBL:CCD54564.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD54564.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; FQ790351; CCD54564.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YSG6; -.
DR STRING; 999810.G2YSG6; -.
DR eggNOG; KOG2068; Eukaryota.
DR HOGENOM; CLU_001793_1_0_1; -.
DR InParanoid; G2YSG6; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0030014; C:CCR4-NOT complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd16618; mRING-HC-C4C4_CNOT4; 1.
DR CDD; cd12438; RRM_CNOT4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034261; CNOT4_RRM.
DR InterPro; IPR039780; Mot2.
DR InterPro; IPR039515; NOT4_mRING-HC-C4C4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12603; CCR4-NOT TRANSCRIPTION COMPLEX RELATED; 1.
DR PANTHER; PTHR12603:SF0; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 4; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF14570; zf-RING_4; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 15..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 120..205
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 202..229
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 202..229
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 231..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..109
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 235..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 85284 MW; CB0EC5F98A09052D CRC64;
MAPQDSFIDE DDDTCPLCVE EFDLSDKNFQ PCPCGYQICQ FCYNNIKNNI NGLCPACRRA
YDEKTIKWKV VTPEEVAQFK ANVQKNAKKK AEIRQKEAQK REVESLNRKH LAGLRVVQKN
LVYVNGLSPS IREDELLQTL RGEKYFGQYG KILKIVVSKS KQNDSGQNFG VYVTFASKLD
AERCITAVNG STNGDRVLRA QLGTTKYCSA YLRNENCTNK NCMFLHEPGD NDDSYSRQDL
SSINSVNSQR PLPTKASSSR TQAQAAPPIQ QAQPLAAAAQ PMAREGSKDD SDNGDGPALP
STANWANRGV QQQRSRRGSH ATSAAAPSPA ISNAIPSAPE AVEEETPELV EDQEESSEEA
SPIEAREPTP SIEDVSHPEK EAFGAELLRS INSDVLSWDG PKIHEDDLAS FPPLFDDHGG
EKRRLMREQQ QEEERLHMEQ ESQADLQSVP EPVEEQEPES GSLQLGGEPE DNGREINQPP
GFQRRQSSQL PIQRGSTNGP FGPSLGQQQN YQNISNLGSV NGRSLTPLQQ SQLSMFKSPS
GVPPSFMDHI SSPVGLGNPL NQNNALFQQP GHNRQSSRYS FAGDGAAGPS SIKPSANSKM
MQQQASMMPP SSHPQQGFQS FNPSIPAPPG LSGLKSNTPP IGGGMFGQGH GFGNTMGGGS
AFGGANKENG SEMLREILRG RPSAGGNQGL DTSKPPASGL LASLYGPQTG AFHDFGQKQK
KKGKKHRHAN TSSSGGGGLV DLADPSILQA RMQHQQQSNA GVGQGLFGQA QGGYNPNLMY
GGGAGFPRW
//
