ID N1QMY6_SPHMS Unreviewed; 798 AA.
AC N1QMY6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SEPMUDRAFT_122813 {ECO:0000313|EMBL:EMF17423.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17423.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF17423.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF17423.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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DR EMBL; KB456260; EMF17423.1; -; Genomic_DNA.
DR RefSeq; XP_016765544.1; XM_016901799.1.
DR AlphaFoldDB; N1QMY6; -.
DR STRING; 692275.N1QMY6; -.
DR GeneID; 27898936; -.
DR eggNOG; KOG2068; Eukaryota.
DR HOGENOM; CLU_001793_1_0_1; -.
DR OMA; CNNRNCM; -.
DR OrthoDB; 1748at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
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; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
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 18..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 123..208
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 205..232
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 205..232
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 246..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 86342 MW; A0778984E896115A CRC64;
MSRSLQDQFI DDDEEETCPL CVEEFDLTDK GFRPCPCGYQ ICQFCYHNVK TNMNGLCPAC
RRPYNDADIE YKLITPEETA AHKARQAHKQ RKTLQALQKE KQKAEADNLS RKHLAGMRVV
QKNLVYVTGL SPTSQEDQLL QTLRGDQYFG QYGKIIKIVV SKAKDPSHPH SVGVYVTYEL
KEDAAACIAA VDGSKNGDRT LRAQFGTTKY CSAYLRGENC TNRNCMFLHE PGEANESYSR
ADLSALNAGS SQQGSARPPP PQSQQPVASA APTMMRQGST DQHAPSPAPD RPALPSTASW
ATKLPQSSRA ESRSTSGTVE SPAPVISIPA AAQPEVAVEQ APLPQATPSQ ETSEDSALPD
FPSARPDSPQ SRRKHISPLD AFLANIKLED FKLVWSDKCL TETEQNMIKS FPPLFDENGG
AKRRLRRQRE EESRRIEQEV QVFQQPPLAE PDDNPEMSGS LQLGGEPEER QGSNQMQSAI
HPPGQDGGVD QRYQYGGVAT SSPGTSDRGL TPQQHQQMLL QTLKPNAPSA FMNNTGQQAT
FNTSFPQQAT NPPHGHQRNV SRYSFANDSA SASTAVKPVA NPKIMNQQAA MMPSTGGNHF
GAQHQQPHGQ FYTSNVQGPP PGLKTTGTPP VSGNLTFGQG HGFATGGLQY GAGSSRNQQD
TYYRDLLRGN NEAAMSGRVE PKRELQSLPS YNNAQSHAAF MATQPNAYPA PSYANLGAFG
DGEKQRKKKG KKHRHADTSS SSGGGMIDVS DPGASHLLPS RMHQGASGFG GGAFAGQAVG
TAGALYSGMH GGGYNGRW
//