ID   CRED_NEOFI              Reviewed;         601 AA.
AC   A1DMJ3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=NFIA_053600;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16014.1; -; Genomic_DNA.
DR   RefSeq; XP_001257911.1; XM_001257910.1.
DR   AlphaFoldDB; A1DMJ3; -.
DR   SMR; A1DMJ3; -.
DR   STRING; 36630.CADNFIAP00004688; -.
DR   EnsemblFungi; EAW16014; EAW16014; NFIA_053600.
DR   GeneID; 4584426; -.
DR   KEGG; nfi:NFIA_053600; -.
DR   VEuPathDB; FungiDB:NFIA_053600; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_2_0_1; -.
DR   OMA; GMATPFH; -.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000006702; 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..601
FT                   /note="Probable HECT-type ubiquitin ligase-interacting
FT                   protein creD"
FT                   /id="PRO_0000395702"
FT   REGION          374..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  66372 MW;  0DA56BBC5509CFAE CRC64;
     MALSFFGGGG ASHLKYFDIR LDEDYIVFRG GEQEAASAQL SGKLLLCLSE PLSAKHVRLN
     LTGISRVCWH LPSSSASGGR KSWREKVFYE KSWTFRDAGK SKTEILAAGN YEFPFHVILE
     GSMPESVEGL SDTYVTYRFK AEIGRKYAKD IVVRKPLRII RTLDSSALEL SHAMSVENIW
     PNKIEYSIST PTKAVIFGTS IRVDFKLIPL LKGLKIGQIV SQLIESHDLT LNPEDPDSVR
     NTYKNTRTIV NDEHELDEEN NLEIIDEAAE GYQFSRFLDL PKTLTRCLQD TDTRGIKIRH
     KLKFRVQLLN PDGHISELRA TLPVSIFISP NLAIDDNNNL VDQTPQSAQR AVNDLAQQAP
     PLYGEHQFDQ LYSEVDPSGY RTPGPGSGPG TPFGTLSRNL SAENLASMNA LTNTDISASA
     LHSRLSNLHA SRFSNPSPAD TDGHTDVEHR RLGVSADYFG PSSGSNSHSP ASPELSRRPS
     DEGYHDHDHI PSGMATPFHP QFAEVESLSR VPSYSTAVRS TVGPCDSELP DYQAVVAEDT
     AMPTLQSPQQ AHIRSAGRGA STGHTGIDVH HLRSGLFNSR TSAHHDDDDR RLRLVQARAR
     V