ID I2H9T1_TETBL Unreviewed; 741 AA.
AC I2H9T1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TBLA0J01370 {ECO:0000313|EMBL:CCH63133.1};
GN ORFNames=TBLA_0J01370 {ECO:0000313|EMBL:CCH63133.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH63133.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH63133.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE806325; CCH63133.1; -; Genomic_DNA.
DR RefSeq; XP_004182652.1; XM_004182604.1.
DR AlphaFoldDB; I2H9T1; -.
DR STRING; 1071380.I2H9T1; -.
DR GeneID; 14498316; -.
DR KEGG; tbl:TBLA_0J01370; -.
DR eggNOG; KOG2068; Eukaryota.
DR HOGENOM; CLU_028046_0_0_1; -.
DR InParanoid; I2H9T1; -.
DR OMA; DGTYMDG; -.
DR OrthoDB; 1748at2759; -.
DR Proteomes; UP000002866; Chromosome 10.
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 GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
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; PF14570; zf-RING_4; 1.
DR SMART; SM00184; RING; 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:UP000002866};
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 34..79
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 138..253
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 250..277
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 250..277
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 101..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 84141 MW; ABD97E373204E4DE CRC64;
MTLNPHVQQN LQNIQKALSN YDMSFLSEDE EDYCPLCLEK LDITDKNFRP CPCGYQICQF
CYNNIRQNEE LNGRCPACRR KYDDETVKYV VLTPEELKYE KEKQSRKDWE KKQREKERKD
NENANRKHLA GMRVIQKNLV YVVGLNPPVP YDEIIPYLKS DKYFGQYGKI NKIVVNRKNN
NNNSGNSNNN NHSNDHYHQN SLPSSSGSNS SSHNQGYGIY ITFSRKEDAA KCIQQVDGTY
IDGRLVKAAY GTTKYCSSYL RGLPCPNPNC MFLHEPGEEA DSFNRRELNN KQHSHNPNSS
LPHLNTNQSL YSSSNNTPTT TTNNNLSNTK SSTTINSTTT THSASPSPAL AKSQLHNSQQ
LNGHSYLDQN NNSLSNTLSN NNTGTSTPIL IPATLPAGSN PWGVTQSATP LTSLNLNKSA
LPTLNDTLSN SNSNLDSQDE ITSLYQQSQQ ASPRQHQTQY DEVQQSPQNS NTTNNNKKKN
VNVEQDYVDP YDVVNNAVTF LDERIHDLSD YKSVKLALKS NILDNETYSR YPSLFTWSHI
EPTKTSKNVL TKKLIEILAI KPVDHTSSVV EFLKENAETI AALNANTAAM LALQQQQAQQ
QQQQQQQQQQ QQQQQQQQQA QQQQQQQAQQ QAQLQQQQLQ QAQLQQQQLK SQLQQQQQLK
KQLQQQQQQQ AQQQQQQQQQ QLRMGMTNAP PPGMFTPQQM PLQLQQQQLA QQQHPNESIP
SNSTDFLNQL INGRRTAAAG N
//
