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Database: UniProt
Entry: A0A2K3PT47_9HYPO
LinkDB: A0A2K3PT47_9HYPO
Original site: A0A2K3PT47_9HYPO 
ID   A0A2K3PT47_9HYPO        Unreviewed;      1553 AA.
AC   A0A2K3PT47;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=General negative regulator of transcription subunit 4 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TCAP_07529 {ECO:0000313|EMBL:PNY18446.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY18446.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY18446.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY18446.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PNY18446.1}.
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DR   EMBL; NRSZ01001313; PNY18446.1; -; Genomic_DNA.
DR   STRING; 45235.A0A2K3PT47; -.
DR   OrthoDB; 1748at2759; -.
DR   Proteomes; UP000236621; Unassembled WGS sequence.
DR   GO; GO:0030014; C:CCR4-NOT complex; IEA:InterPro.
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; 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; 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; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          15..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          121..207
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          82..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..846
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..949
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1553 AA;  164266 MW;  2743BA2ED0F556D0 CRC64;
     MASQDSFLDE EEDCCPLCIE EFDVYDRSFR PCPCGYQVCQ FCWNNIKTNM NGLCPACRRP
     YDEKPTKWKV VTQEEVAQFN ANIQRSQRKR AQEQRQKEAQ KRETEKETRK SLVGVRVVQK
     NLVYITGLAP TIREDELLKT LRKHEFFGQY GSIQKISISN RKSSDGQHHS LGIYVTFEKP
     EEATRCIQAV HGSQNGDRIL KAQHGTTKYC SAWLKNEKCI NPGCMFLHEQ GEEEDSYTRQ
     DLSSMNSIHT QRPLPGGAGT SSRSVSRQQV SQPTSPPASQ PMARSLSKEG SENGVDTSAL
     PLSANWARNP QRSRRGSHAT SGAASSPAIS TSLPVTAEAV QEAVEDTASL ASTHAAAKAK
     QSEGAASDER RRPTEDPELT ELLNAMGRLA MPKPDLELAN SLPPLFDMRG GAKRRAMREA
     EKARVRDPED RSETHVPSDG EPEMGGGSLA LGGEPEEREV SADAHGFDQR QGGAQPPIQR
     RSTDGLFGAA LGGSGFGQGP TNPMGRAMTP QQLASLRSQG GFGEQMPPGI SNHSNMFQTQ
     GHNRQSSRFS FANDNPNSAT NVKLAANPRI MAQQSSMMPS SFQSQGGNXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXVA PPPGLKSTGT PPSMFGQSFG GSGFGAAPKD
     SSNDLLQGYI GRSRGGGNPP HDAGKREYMI SSFSDQYPPP STSTPAPASG LLASLYGNHP
     GAFQDFGSKQ KKKGKKHRHA NTSSSGGSGL VDLADPSILQ ARMQHQPQSN AGVGQGLFGG
     GQSQDDELLS LDEATNSVDA LVSDEPRGVF ARPGLYSAMG AGPLAPPGFA APPGEPETPL
     KPSTAPGRPR PANIVPVVPK IPPPGLDRGA VTPEQTPRKV APGSETRKNI KSLVVDSGLA
     TTGLSQPRPG QLRAAIALQD EDFPALNAPK ARKQPPASPA IPAVPTPNGT PAPKKSSSDR
     GSETATEKPN NNPAAAPTQP IESGHRKQGA GNPQPSKAAV SGAEDSIKTT GSADPSAVFP
     FPPLLMPSAA RTTSPAPRAA PKTIRVMPTA RTEVALPSPA QSVASKAVST SYRPGTPGSE
     INSDTASVLS ASVSASRAGS PPPSKIGSAA IRSTTKSQQR KQRKEATKQE TKTIAGAPKS
     EAEEHAPVLG RKKKQKKEKS ATATTAQTRA DAPAQGPVKG EEPASAGAQK EDGRGKDSDD
     ADLKAKATSI NKSAKGKEKE KEKEKSATVP SQPPPPETTS APQTAEPEKP QPGPVSVFAE
     IRDSLWTTAV EALLMLRPVA SSSSRQDHGN NNAQSNKTGY CKDCACKCGE IHDDDLAALR
     AGRPVRKQFH VDGSRMLITP NGDCIRGLTP EEEDAFLDLQ AAIAATAENP GAFVAPRHQP
     GSGAFSLIKG RAVPNGRPNI FPATSQPQSQ DPIGKLQRED ALSYINQYVL PRLNLGASNM
     GFPKGASPAR DSAAASLNSL APYFYGPDAA AGVGIYSAPD GARAMQDFAS SGVAQGDEAG
     KMPGASGIGG IPLMSVEDAE MALTTARKET EKLEKGLNAV IKRNRRLLLG SGN
//
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