ID G4U9R8_NEUT9 Unreviewed; 466 AA.
AC G4U9R8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=RING-Gid-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE2DRAFT_146609 {ECO:0000313|EMBL:EGZ76937.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76937.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ76937.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL890999; EGZ76937.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U9R8; -.
DR STRING; 510952.G4U9R8; -.
DR eggNOG; KOG2817; Eukaryota.
DR HOGENOM; CLU_020227_0_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16652; dRING_Rmd5p-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170:SF3; GH10162P; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 220..277
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 411..452
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 411..452
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT REGION 151..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 52175 MW; 1028042F26148115 CRC64;
MTAQTTAMEA LQKELDRLNR APGLSATEDR VDKIIEMLTS VKDQIVQSGM DTHVASMSIT
RIQNPIKSTF EKINDDLKGV TATQRKLGKT LDKHFPLKDL PSTHDAMADQ ESLINRAISM
HLLREGQFSV ASTFIEETGD AATLENVNAV VEGQDQVSAS DNYDDEPMDD DRDDDDDDED
DDDDDDEDEY MSPLEGAATG LGFRQLQNLS SLQSHELEAK FSQMYTILQD IKSRNLLSAI
EWARSNSGEL EARGSNLEFE LSRLQYVWLF KGPRVNGLPD NELNGTAGAL LYAQQNFWRF
GNRYIGEIQQ LANAQIYARN LSESPYRHIF STETAFADVA SSFTREFCSL LGLSAESPLY
VAVTAGALAL PLLIKYQQAT RAKGTEWTTT NELAFETPLP ERMLYHSIFV CPVSKEQTTE
QNPPMMIPCG HVLAKETLQR LLKGTRFKCP YCPAEGLEKD ARRIMI
//
