ID   CRED_EMENI              Reviewed;         597 AA.
AC   Q6SIF1; C8V4P2; Q5B5L0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; Synonyms=cre-34; ORFNames=AN4170;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH HULA.
RX   PubMed=15255903; DOI=10.1111/j.1365-2958.2004.04172.x;
RA   Boase N.A., Kelly J.M.;
RT   "A role for creD, a carbon catabolite repression gene from Aspergillus
RT   nidulans, in ubiquitination.";
RL   Mol. Microbiol. 53:929-940(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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       {ECO:0000269|PubMed:15255903}.
CC   -!- SUBUNIT: Interacts with hulA. {ECO:0000269|PubMed:15255903}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; AY458430; AAS10351.1; -; Genomic_DNA.
DR   EMBL; AACD01000067; EAA59431.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF74562.1; -; Genomic_DNA.
DR   RefSeq; XP_661774.1; XM_656682.1.
DR   AlphaFoldDB; Q6SIF1; -.
DR   SMR; Q6SIF1; -.
DR   STRING; 162425.CADANIAP00004501; -.
DR   EnsemblFungi; CBF74562; CBF74562; ANIA_04170.
DR   EnsemblFungi; EAA59431; EAA59431; AN4170.2.
DR   GeneID; 2873587; -.
DR   KEGG; ani:AN4170.2; -.
DR   VEuPathDB; FungiDB:AN4170; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_2_0_1; -.
DR   InParanoid; Q6SIF1; -.
DR   OMA; GMATPFH; -.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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; IGI:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP: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   1: Evidence at protein level;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..597
FT                   /note="HECT-type ubiquitin ligase-interacting protein creD"
FT                   /id="PRO_0000395701"
FT   REGION          375..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65956 MW;  052ED116FE641B90 CRC64;
     MALSFFSGGG SASHAKYFDI RLDEDYIVFR GGEQEAASAH LSGKLVLCVS EPISIKHIRL
     HLTGISRVCW HLPSSSAGGG RKNWRERVFY EKTWKFRDAG KSKTEILPAG NYEYPFDVIL
     EGSMPESVEG LSDTYVTYRF KAEIGRKYAK DIVVRRPLRI IRTLESSALE LSHAMSVENI
     WPNKIEYSIS TPTKAVIFGT SIRVDFKLIP LLKGLGIGQI ISQLIETHDL TLNPEDPDAI
     RNTYKTTRTI INDEHTIDEE NSLEIIDEAA EGFQFSRTLD LPKTLTRCLQ DTDTRGIKVR
     HKLKFRVQLL NPDGHISELR ATLPVSIFIS PNLAIDDNNN LVDSSPQTTQ RALDDLAQQA
     PPLYGEHQFD QLYSEVDPSG YRTPGPGSGP GTPFGTLSRN LSAENLASMN AITHTDISAS
     ALHHRLVNLD LRGHGRVSAS EHDHLGVPSD NGPPSGSNTH GSNTHAPGSP ELSRRASDED
     VHDNIPSGMA TPFIPHSAEL ETLSRVPSYS TAVRSSVRPH DSDLPDYQAV VAETVHMSAP
     QSPQQAHIRG SGTGRGSDSY FSAPMDFFHR PAFLHSRSHS HSDDERRIRL TQARGRA