FYV10_EMENI
ID FYV10_EMENI Reviewed; 406 AA.
AC Q5AS80; C8V9H9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein fyv10;
GN Name=fyv10; ORFNames=AN8850;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=CBF77885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA60138.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000163; EAA60138.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF77885.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_682119.1; XM_677027.1.
DR AlphaFoldDB; Q5AS80; -.
DR SMR; Q5AS80; -.
DR STRING; 162425.CADANIAP00006203; -.
DR EnsemblFungi; EAA60138; EAA60138; AN8850.2.
DR GeneID; 2868352; -.
DR KEGG; ani:AN8850.2; -.
DR VEuPathDB; FungiDB:AN8850; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_2_0_1; -.
DR InParanoid; Q5AS80; -.
DR OrthoDB; 1087488at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR006594; LisH.
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 SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 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..406
FT /note="Protein fyv10"
FT /id="PRO_0000292459"
FT DOMAIN 126..158
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 164..221
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 329..391
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 406 AA; 46596 MW; 1A9106DA31D73353 CRC64;
MAAELTSTKL NAENHLLLDQ PLLRLPHELA RRNLKSFQRI VEREKEYVLP ALKEAAKASM
SGNQTPEQTL ATLDVMISRM QGLKRKMENL QQEEKKIHHQ SRKRIQHLNQ LYQIPSLTDV
KYDQWSRVRL DRLVIDHMLR SGYSESAQRL ARAKNIEELV DLNVFVQCQR IAESLRNGET
KDALQWCNEN KAALKKSQYN LEFELRLQQY IEMIRTRDRA KFVDAMVHAR RYLAPYDETQ
SAEIRRAAGL LAFPPNTRAE PYKSMYASER WVYLSELFIR THHELLSLPS RPLMHIALSA
GLSALKTPAC HSAYTSSSSN SHSTATSVCP ICSTELNELA RNLPYANHTK SSVENDPVVL
PNGRVYGLHR LLDMSKKLSS LEAGKVRDPT TGEIFNESEL KKVYIM