GRRA_EMENI
ID GRRA_EMENI Reviewed; 585 AA.
AC C8V4D4; Q15I80; Q5B5I0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=SCF E3 ubiquitin ligase complex F-box protein grrA;
DE AltName: Full=F-box and leucine-rich repeat protein grrA;
DE AltName: Full=F-box/LRR-repeat protein grrA;
DE AltName: Full=SCF substrate adapter protein grrA;
GN Name=grrA; Synonyms=grr1; ORFNames=AN10516;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND LEUCINE-RICH REPEATS.
RX PubMed=16824096; DOI=10.1111/j.1365-2958.2006.05215.x;
RA Krappmann S., Jung N., Medic B., Busch S., Prade R.A., Braus G.H.;
RT "The Aspergillus nidulans F-box protein GrrA links SCF activity to
RT meiosis.";
RL Mol. Microbiol. 61:76-88(2006).
RN [2]
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 [3]
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 meiosis and required for ascospore formation.
CC Involved in substrate recognition in ubiquitin-dependent degradation.
CC {ECO:0000269|PubMed:16824096}.
CC -!- SUBUNIT: Part of a SCF E3 ubiquitin ligase complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16824096}. Note=In
CC the cytoplasm of ascogenous cells. Within these cells, defined areas
CC that resembled immature ascospores were excluded from the staining.
CC -!- TISSUE SPECIFICITY: Specifically expressed in ascus mother cells.
CC {ECO:0000269|PubMed:16824096}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during hyphal growth in
CC liquid culture. Slightly elevated expression when asexual sporulation
CC is induced. A significant rise can be detected following the
CC developmental sequence of cleistothecia development, which is
CC accompanied by the differentiation of Huelle cells and eventually
CC ascospore formation. This increase coincides with the intermediary
CC phase of the developmental pathway, starting after 72 hours post
CC induction to result in peak levels at approximately 120 hours after the
CC onset of differentiation. {ECO:0000269|PubMed:16824096}.
CC -!- INDUCTION: During ascospore formation within the cleistothecium.
CC {ECO:0000269|PubMed:16824096}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA59299.1; Type=Erroneous gene model prediction; Note=The predicted gene AN4200 has been split into 2 genes: AN10516 and AN10522.; Evidence={ECO:0000305};
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DR EMBL; DQ309327; ABC25061.1; -; Genomic_DNA.
DR EMBL; AACD01000068; EAA59299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF74496.1; -; Genomic_DNA.
DR AlphaFoldDB; C8V4D4; -.
DR SMR; C8V4D4; -.
DR STRING; 162425.CADANIAP00004464; -.
DR EnsemblFungi; CBF74496; CBF74496; ANIA_10516.
DR EnsemblFungi; EAA59299; EAA59299; AN4200.2.
DR VEuPathDB; FungiDB:AN10516; -.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_003436_0_0_1; -.
DR InParanoid; C8V4D4; -.
DR OMA; LCNRIRY; -.
DR OrthoDB; 1282076at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IGI:AspGD.
DR GO; GO:0030437; P:ascospore formation; IMP:AspGD.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00367; LRR_CC; 12.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Leucine-rich repeat; Meiosis; Reference proteome; Repeat;
KW Sporulation; Ubl conjugation pathway.
FT CHAIN 1..585
FT /note="SCF E3 ubiquitin ligase complex F-box protein grrA"
FT /id="PRO_0000273528"
FT DOMAIN 65..113
FT /note="F-box"
FT REPEAT 147..171
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 172..197
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 198..223
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 224..249
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 250..275
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 276..301
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 302..329
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 330..355
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 356..381
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 382..407
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 408..432
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 433..465
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REPEAT 466..491
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:16824096"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65081 MW; A0FA8E1BBEDF65EC CRC64;
MARSRQPTRF SSEAPSESSS STSPERAADD DTDFFTLQAN DSQSSIGAGN PRDSHIQNDP
ETVLPPIAYL PPEILISIFS KLSSPRDLLS CLLVCRIWAL NCVGLLWHRP SCNNWDNLKK
IAAAVGEEDS FFLYSSLIKR LNLSALTEDV SDGTVVPFSQ CNRIERLTLT NCRKLTDIGV
SDLVVGSRHL QALDVSELRS LTDHTLFKVA ENCNRLQGLN ITGCVKVTDD SLIAVSQNCR
LLKRLKLNGV SQVTDKAILS FAQNCPSILE IDLQECKLVT NQSVTALMTT LQNLRELRLA
HCTEIDDSAF LDLPRHIQMT SLRILDLTAC ENIRDEAVER IVSSAPRLRN LVLAKCKFIT
DRAVWAICKL GKNLHYVHLG HCSNINDSAV IQLVKSCNRI RYIDLACCSR LTDRSVQQLA
TLPKLRRIGL VKCQLITDAS ILALARPAQD HSVPCSSLER VHLSYCVNLT MVGIHALLNS
CPRLTHLSLT GVAAFLREEL TVFCREAPPE FTRQQREVFC VFSGEGVNRL RNHLNREAAP
QRDANEATMY DDEEELDEDE GQVTGLMHAA AINDDDYINI TPPHA
