ID A0A2K3QKF5_9HYPO Unreviewed; 434 AA.
AC A0A2K3QKF5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE SubName: Full=Regulator of gluconeogenesis Rmd5 {ECO:0000313|EMBL:PNY28017.1};
GN ORFNames=TCAP_02059 {ECO:0000313|EMBL:PNY28017.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY28017.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY28017.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY28017.1,
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:PNY28017.1}.
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DR EMBL; NRSZ01000316; PNY28017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QKF5; -.
DR STRING; 45235.A0A2K3QKF5; -.
DR OrthoDB; 208500at2759; -.
DR Proteomes; UP000236621; 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; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
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 SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50089; ZF_RING_2; 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:UP000236621};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 188..245
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 379..420
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT DOMAIN 379..420
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 379..420
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT REGION 141..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 49030 MW; 1A4117114EB637D2 CRC64;
MAGPDDDTAS PFAPLLVELA RMRKSNLTAA IRDVDQIISL LMSAREQVAA DADAHRIGMA
MTTLQNPVKA QMEAITNDLK DVTKAQKGFG KALDKALPQR ELPMETDAMA DHPLLIDRAI
AMHLLREGQF SVASTFLREE QEQRRQNAST TAMTHTISRV DEDGDDEMKR DDEADTDMQS
LSEDLQDKFS EMYSILAELK ERNLTPAIEW ARINNPRLEA NGSNLEFELC KLQFVWLFKG
HSQNGLPDDD HNGQLGALAY ARKHFARFQS RHLKEVQQLC CAMIYATNLE ESPYHHIFEI
NSAFEDVATS FTREFCSLLG LSAESPLYIA VTAGSIALPR LIKYTTYMKE KKTEWTTENE
LAFETPLPQS MVYHPIFVCP VSKEQTTEQN PPMILPCGHV ICRESLHKIT KGSRYKCPYC
PTEGHLRDTM QITL
//
