FYV10_PICST
ID FYV10_PICST Reviewed; 511 AA.
AC A3LPW2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Protein FYV10;
GN Name=FYV10; ORFNames=PICST_55076;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- FUNCTION: Involved in the proteasome-dependent degradation of fructose-
CC 1,6-bisphosphatase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FYV10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000496; ABN64567.2; -; Genomic_DNA.
DR RefSeq; XP_001382596.2; XM_001382559.1.
DR AlphaFoldDB; A3LPW2; -.
DR SMR; A3LPW2; -.
DR STRING; 4924.XP_001382596.2; -.
DR EnsemblFungi; ABN64567; ABN64567; PICST_55076.
DR GeneID; 4837192; -.
DR KEGG; pic:PICST_55076; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR InParanoid; A3LPW2; -.
DR OMA; IKLEMIR; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR027714; Fyv10/MAEA.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
DR Pfam; PF10607; CLTH; 1.
DR SMART; SM00757; CRA; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..511
FT /note="Protein FYV10"
FT /id="PRO_0000292465"
FT DOMAIN 201..259
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 430..496
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT REGION 112..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 59773 MW; D17EC24D0EC641AA CRC64;
MSEPSLNFHI QSHSTQFRIP TELIKKNFKT IQKLVEKQKK QMTDDVAKIK KNPNIPTAMK
LAMVRKSIKS FEGFQKKLQA SIAKDEELRS RLIARIEHLA LISEYCITQD KTKTQVEKPS
QPQSQNEDTE EKEHSTKDDN DKYLDLHNPN LITWYRDQTN LLIIDYLIKS NTRTDHNIGL
LLLKSLSESN PKYMKLIDYD LFESFNKVYV SIMEDHDLTL VIAWFNENRN FLKKANSNLE
FEINYCRFLS LIEKGDVNEA IKFSSINLSP YGNVSNYQDT DRANHEHNLN RLKEIGGLLV
YMAINEEKRT RNDKIAFSSN LLINSPRFHE YEKLLSDERW DSLSMCFVEN FTKLYGISKN
YPIFIYLSAG LASLKTKSCY HNTENTIFRE NQEINVTDES IYKKDLTVLT DKKYRGSNQY
YKLLNKINNC PVCSPELYKL SRNLPYAQLI TSIFNNPFKL PNGNIYPFDK LLNPSEKYLS
EKNTLLRMGK IKDPLTREIF LIDTCIRVYP A