DIA2_ASHGO
ID DIA2_ASHGO Reviewed; 685 AA.
AC Q75A03;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein DIA2;
GN Name=DIA2; OrderedLocusNames=ADR230W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 69-70 AND 80.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: F-box protein component of a SCF ubiquitin ligase complex
CC involved in ubiquitin-dependent protein degradation. The SCF-DIA2
CC complex is specifically involved in the pheromone induced degradation
CC of phosphorylated TEC1. Involved in DNA replication, genome stability,
CC and the control of cell cycle, probably through its association to
CC replication origins to facilitate the ubiquitination of another origin-
CC binding protein (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a SCF ubiquitin ligase complex which binds to DNA
CC replication origins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DIA2 family. {ECO:0000305}.
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DR EMBL; AE016817; AAS52150.2; -; Genomic_DNA.
DR RefSeq; NP_984326.2; NM_209679.2.
DR AlphaFoldDB; Q75A03; -.
DR SMR; Q75A03; -.
DR STRING; 33169.AAS52150; -.
DR EnsemblFungi; AAS52150; AAS52150; AGOS_ADR230W.
DR GeneID; 4620488; -.
DR KEGG; ago:AGOS_ADR230W; -.
DR eggNOG; ENOG502QRSD; Eukaryota.
DR HOGENOM; CLU_023422_0_0_1; -.
DR InParanoid; Q75A03; -.
DR OMA; ISCKGYL; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Cell cycle; Leucine-rich repeat; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..685
FT /note="Protein DIA2"
FT /id="PRO_0000233002"
FT REPEAT 6..39
FT /note="TPR 1"
FT REPEAT 70..103
FT /note="TPR 2"
FT REPEAT 104..137
FT /note="TPR 3"
FT DOMAIN 207..254
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 300..323
FT /note="LRR 1"
FT REPEAT 353..377
FT /note="LRR 2"
FT REPEAT 454..480
FT /note="LRR 3"
FT REPEAT 499..517
FT /note="LRR 4"
FT REPEAT 518..542
FT /note="LRR 5"
FT REPEAT 562..585
FT /note="LRR 6"
FT REPEAT 598..622
FT /note="LRR 7"
SQ SEQUENCE 685 AA; 79100 MW; 8CB95476C40EFA3A CRC64;
MSEDIIDRSL ELGIQCFQGE DYKGAAELFS KSLQLARSYT DRSLEGIREK VGLPKRCLHD
PSRVYHPRYL VLLDNRAATW EKLNKLDRAL ADAAYMITVD AYNLKGYIRR GKVLQKLGRY
EEALQVYENG LKQAGEAEKT HAIHAPQKFL DIVYRQRSTI KELLQSRARS SRSLTQQTVA
KEPKLKRPAT IDSLMPGKKR SSSKAKIDYI ATLPVEIIER IMANMDTRSI IRCYSVCKLW
KYRLERLPHL YQEFRLSCCY KNMLGYVNFV GALASRTAEY SCRSIQCVSG NVQEEEKSII
LLLSRLMIGT RQLALMAKKC KAERIIQHIC ENKKLRNGVQ RLSITAPVHF GHKLNLHELY
TRTTSMTHLE LVLNFHTPSE HVGGHLFPWQ DHAVAETNLE SFTLMARNYS VHHVNVIEQF
EYSSVLFKRL KKLCITGIDF RLGDRNNLKW ISDMPNLQEL WLERNTGIEF HELITQIVQV
GAPKTLRHLT FREPPNRHFD RMDQSQLGLG EEALREVFQS LESLDLMNTR FDPQLLLLLL
QPACENRIAR LNIGNCPRLS FARDLEILTL IFQQLPALTD LLLPNVMEYT RQGMEVLRKN
IKGMKLKRLD LSFIPSLKGY ELLDLLKELK GINPLGLETL TINGCTAVAP QTVDYITRNG
YAQKVMCAYE RTQWEHLGIN SFWYR