ID   CRED_ASPFN              Reviewed;         603 AA.
AC   B8N4G0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=AFLA_036630;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Component of the regulatory network controlling carbon source
CC       utilization through ubiquitination and deubiquitination involving creA,
CC       creB, creC, creD and acrB. May be involved in signaling by recognizing
CC       appropriately phosphorylated substrates via its arrestin domains and
CC       then recruit a HECT-type ubiquitin ligase such as hulA, leading to
CC       ubiquitination of the substrate, providing a link between
CC       ubiquitination and phosphorylation in protein regulation and stability
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with hulA. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arrestin 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; EQ963473; EED56391.1; -; Genomic_DNA.
DR   RefSeq; XP_002375173.1; XM_002375132.1.
DR   AlphaFoldDB; B8N4G0; -.
DR   SMR; B8N4G0; -.
DR   STRING; 5059.CADAFLAP00003038; -.
DR   EnsemblFungi; EED56391; EED56391; AFLA_036630.
DR   VEuPathDB; FungiDB:AFLA_036630; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_2_0_1; -.
DR   OMA; GMATPFH; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; ISS:UniProtKB.
DR   Gene3D; 2.60.40.640; -; 1.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ubl conjugation pathway.
FT   CHAIN           1..603
FT                   /note="Probable HECT-type ubiquitin ligase-interacting
FT                   protein creD"
FT                   /id="PRO_0000395697"
FT   REGION          375..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  67103 MW;  BCC60D188DBA4AB9 CRC64;
     MALSFFSGGG SASHAKYFDI RLDEDYIVFR GGEQEAASAH LSGKLLLCLS EPLSIKHIRL
     HLTGISRVCW HLPSSSAGGG RKSWRERVIY EKTWRFRDPG KGKTEILPAG NYEYPFNLVL
     EGNMPESIEG LSDTYITYRF KAEIGRKYAK DIIVRKPLRI IRTLEPSALE LAHAMSVENI
     WPNKIEYSIS TPTKAVIFGT SIRVDFKLIP LLKGLTIGQI VSQLIESHDL TLNPEDPDSI
     RNTYKNTRTI LNDEFELDHD NALEIIDEAA EGYQFSRYLD LPKTLTRCLQ DTDTKGIKVR
     HKLKFRVQLM NPDGHISELR ATLPVSIFIS PNLAIDENNN LVDQTPQSAQ RAINDIAQQA
     PPLYGEHQFD QLYSELDPNG YRTPGPGSGP GTPFGTLSRN LSAENLASMN ALTNTDISAS
     ALHSRLSNLS NLNITRPHQP SPTDHESQND SEHRRLGVPA DYFGPSSGSN SHSPSSPVLS
     RRPSDEVDHE HVPSGMATPF HPQYAEVETL SRVPSYSTAV RTTVRPHDSD LPDYDAVVAE
     DIPVPPPLQS PQQAHIRNAG RGSSQLFSSL DILHHRPGLG HSHSSSHDDE DRRLRLVQAR
     ARV