ID   CRED_ASPFU              Reviewed;         601 AA.
AC   Q4WN21;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=AFUA_6G07900;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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}.
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DR   EMBL; AAHF01000006; EAL88643.1; -; Genomic_DNA.
DR   RefSeq; XP_750681.1; XM_745588.1.
DR   AlphaFoldDB; Q4WN21; -.
DR   SMR; Q4WN21; -.
DR   STRING; 746128.CADAFUBP00007196; -.
DR   GeneID; 3508824; -.
DR   KEGG; afm:AFUA_6G07900; -.
DR   VEuPathDB; FungiDB:Afu6g07900; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_2_0_1; -.
DR   InParanoid; Q4WN21; -.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IBA:GO_Central.
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_0000395698"
FT   REGION          374..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  66388 MW;  75694E26A6B84798 CRC64;
     MALSFFGGGG ASHLKYFDIR LDEDYIVFRG GEQEAASAQL SGKLLLCLSE PLSVKHVRLN
     LTGISRVCWH LPSSSATGGR KSWREKVFYE KSWTFRDAGK SKTEILAAGN YEFPFHVILE
     GSMPESVEGL SDTYVTYRFK AEIGRKYAKD IVVRKPLRII RTLDSSALEL SHAMSVENIW
     PNKIEYSIST PTKAVIFGTS IRVDFKLIPL LKGLKIGQIV SQLIESHDLT LNPEDPDSVR
     NTYKNTRTIV NDEHELDEEG NLEIIDEAAE GYQFSRFLDL PKTLTRCLQD TDTRGIKIRH
     KLKFRVQLLN PDGHISELRA TLPVSIFISP NLAIDDNNNL VDQTPQSAQR AVNDLAQQAP
     PLYGEHQFDQ LYSEVDPSGY RTPGPGSGPG TPFGTLSRNL SAENLASMNA LTNTDISASA
     LHSRLSNLHA SRFSNPSPSD ADGHTDAEYR RLGVSTDSFG PSSGSNSQSP ASPELSRRPS
     DEGYHDHDYI PSGMATPFHP QFAEVESLSR VPSYSTAVRS SVGPCDSELP DYQAVVAEDT
     AMPTLQSPQQ AHIRSVGRGV STGHTGIDVH HLRSGFFNSR TSAHHDDDDR RLRLVQARAR
     V