ID A0A1V9Z4D3_9STRA Unreviewed; 437 AA.
AC A0A1V9Z4D3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=CCR4-NOT transcription complex subunit 4 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=THRCLA_08596 {ECO:0000313|EMBL:OQR92854.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR92854.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR92854.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR92854.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR92854.1}.
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DR EMBL; JNBS01002295; OQR92854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z4D3; -.
DR STRING; 74557.A0A1V9Z4D3; -.
DR OrthoDB; 1748at2759; -.
DR Proteomes; UP000243217; 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; 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; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
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 9..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 110..194
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 66..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 437
FT /evidence="ECO:0000313|EMBL:OQR92854.1"
SQ SEQUENCE 437 AA; 48492 MW; B9B81BC5E5C2811A CRC64;
MAEEEADCCP LCMEELDLTD KTFNACTCGY QVCLWCWHQI KNEYNGLCPA CRAPYSEVAK
QKGAIDREEV IRRTKQREQK KRDQKKSSTA PKVQPVNRRN LANVRVMQRN LVYVIGLPYH
YADDELLRSQ ECFGQYGRIV KAVVNKSHMN SERNGSTASA YITFQNKTDA QNCIDLIDGY
ILDGSLLRAS FGTTKYCNFF LRNLVCNNPE CLYLHELGET DDSFTKEEMA TDFVAGKGCF
RDLTGYDDRR GSAFPPLSQL NIGVEAAKAP ASSDAQRKAQ SAAAVYKLKS QAPENRPKSP
LRAPAPAPTT MSPKDEQPKN PSEKASPTSS AASPVASPPK EASVPQGKPS LYVDTSQSPT
KQDTNSTPLW SQPFPLMQPS PTEQERPINH VFSPFGMGFD GGIHRNTQQA PEYENRKMPP
EPPSNGHVSA WSFEAAS
//