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CRED_ASPCL
ID   CRED_ASPCL              Reviewed;         602 AA.
AC   A1CTF4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Probable HECT-type ubiquitin ligase-interacting protein creD;
DE   AltName: Full=Carbon catabolite repressor D;
GN   Name=creD; ORFNames=ACLA_082820;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW06591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS027060; EAW06591.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001268017.1; XM_001268016.1.
DR   AlphaFoldDB; A1CTF4; -.
DR   SMR; A1CTF4; -.
DR   STRING; 5057.CADACLAP00007775; -.
DR   GeneID; 4699988; -.
DR   KEGG; act:ACLA_082820; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000006701; 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..602
FT                   /note="Probable HECT-type ubiquitin ligase-interacting
FT                   protein creD"
FT                   /id="PRO_0000395695"
FT   REGION          375..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  66767 MW;  F5C7FBC849A0B053 CRC64;
     MALSFFSGGG SASYAKYFDI RLDEGYIVFR GGEQEAASAQ LSGKLLLCLS EPLAAKHVRL
     NLTGISRVCW HLPSGSASGS RKSWREKVFY EKTWTFRDAG KSKTEVLAAG NYEFPFHVIL
     EGSMPESVEG LSDTYVTYRF KAEIGRKYAK DIVVRKPLRI IRTLESSALE LSHAMSVENI
     WPNKIEYSIS TPTKAVIFGT SLRVDFKLIP LLKGLKIGQI VSQLIESHDL TLNPEDPDSI
     RNTYKSTRTI VSDEYELDDE GSLEIIDEEA EGYQFSRYLD LPKTLTRCLQ DTDTRGIKIR
     HKLKFRVQLL NPDGHISELR ATLPVSIFIS PNLAIDENNN LVDQTPQTAR RAVDDIAQQA
     PPLYGEHQFD QLYSEVDPSG YRTPGPGSGP GTPFGALSRN ISSENLASMN ALTSTDLSVS
     ALQTRLSNLH ASRFSNPSPT EIDNHADSEQ RRLGISTADY FGPSSGSNSH SPASPELSRR
     PSDEGYRDHD HIPSGMATPF HPQYAEVETL SRVPSYSTAM RSTVRPCDSE LPDYQAVVAE
     DTAMPALQSP QQAYIRSAGR GTSMNTGIDV HQLRSGHFSS RTSNSHDEED RRLRLVQARA
     RV
 
 
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