ID   CRED_ASPOR              Reviewed;         597 AA.
AC   Q2UM46;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=AO090003000144;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE57369.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007155; BAE57369.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2UM46; -.
DR   SMR; Q2UM46; -.
DR   STRING; 510516.Q2UM46; -.
DR   OMA; GMATPFH; -.
DR   Proteomes; UP000006564; Chromosome 2.
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   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..597
FT                   /note="Probable HECT-type ubiquitin ligase-interacting
FT                   protein creD"
FT                   /id="PRO_0000395699"
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   597 AA;  66412 MW;  5E1B2B5060EC8FF5 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 RTTKTFPFRH LSSHLSKPIS
     EMLGADLANS SLPWIFFIIG RALVTLTPLV TMMKTEDCDS FKLGLESRIR TEAASPA