ID   CRED_ASPTN              Reviewed;         577 AA.
AC   Q0CKB5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=ATEG_05869;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH476601; EAU33630.1; -; Genomic_DNA.
DR   RefSeq; XP_001215047.1; XM_001215047.1.
DR   AlphaFoldDB; Q0CKB5; -.
DR   SMR; Q0CKB5; -.
DR   STRING; 341663.Q0CKB5; -.
DR   EnsemblFungi; EAU33630; EAU33630; ATEG_05869.
DR   GeneID; 4321731; -.
DR   VEuPathDB; FungiDB:ATEG_05869; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_2_0_1; -.
DR   OMA; GMATPFH; -.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000007963; 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   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..577
FT                   /note="Probable HECT-type ubiquitin ligase-interacting
FT                   protein creD"
FT                   /id="PRO_0000395700"
FT   REGION          376..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  64190 MW;  AF17D32044ED9396 CRC64;
     MALSFFGGGG SASHAKYFDI RLDEDYIVFR GGEQEAASAH LSGKLILCLS EPLSIKHIRL
     HLTGISRVCW HLPSSSAGGG RKSWRERVFY EKTWRFREPG KGKTEILPAG NYEYPFNIVL
     EGSMPESVEG LSDTYVTYRF KAEIGRKYAK DIVVRRPLRI IRTLEPSALE LSHAMSVENI
     WPNKIEYSIS TPTKAVIFGT SIRVDFKLIP LLKGLKIGQI VSQLIESHDL TLNPEDPDSI
     RNTYKNTRTI INDEYELDAD NALEIIDEAA EGYQFSRFLD LPKTLTRCLQ DTDTKGIKIR
     HKLKFRVQLL NPDGHISELR ATLPVSIFIS PNLAIDDNNN LVDQTPQTAQ RAVDDLAQQA
     PPLYGEHQFD QLYSELDPAG YRTPGPGSGP GTPFGTLSRN LSAENLASMN ALTTTDISAS
     ALHSRLSNLH ASRHSNPSPS ESENQLESRL GVPTDYFGPS SGSNTHSLTS PELSRRPSDE
     VDHDHVPSGM ATPFHPQYAE VETPEPCPKL FHSGPHFSED VAIPAPQSPQ QAHVRSANRS
     SSYFNPMDLL HHRPGYPGGH GDEEERQLRL MQARARV