ID S7ZMX7_PENO1 Unreviewed; 836 AA.
AC S7ZMX7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN ORFNames=PDE_06989 {ECO:0000313|EMBL:EPS32030.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS32030.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS32030.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family.
CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC ECO:0000256|RuleBase:RU003829}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB644414; EPS32030.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZMX7; -.
DR STRING; 933388.S7ZMX7; -.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR OrthoDB; 5474206at2759; -.
DR PhylomeDB; S7ZMX7; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF168; CULLIN-3; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 455..702
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 96345 MW; 17D223683A65FA50 CRC64;
MASMRARNKI RAPRRSPASA PTDDFDTIWK VLASSLTGIH TKNASSLSFE ELYRNAYRIV
TLSRGHELYQ LVKALERDWL YNHVRCQVAE SILPILLRAE NWQDGSRVVQ DQSNERRAAG
ERFLSVLKET WQDHLVCMGM ITDVLMYMDR TVSVDRSNPS IFVTSMALFR DNVLRVPVRP
DSPTTVANVL ESTVLFLIQL ERDGHMIDRP LIRKCVNMLE GLYETIVEEE TEKLYVTTFE
PQFLNASVAF YQKEGTRLLE EGDAMTFCRQ TLKRIAEEEE RCNVTLAPGT KSKINEVIDR
ELISPNIGEV VRMEGTGVRH MLDQKQFDGL RDLYMLNARV DGKKSVLTQE VRARIVELGQ
AINTMSLAPP PDPTQATNSA NLDSTKRTKD QKKEKSAEKE RPVNAQTASA IKWVDEILAL
KRQFDNVWLH SFQSDQTLLK SIDDSFGEFI NRNIRSSEFL SLFFDENLKK GVKGKTEDEV
DALLDNGILL LRYIKDKDLF ETYYKKHLAR RLLMKKSASM DAERQMISKM KMEVGNQFTQ
RIEAMFKDMT ISQDLTTSYK QHMSRTNAAD DDRPDLEVHV LTSTMWPLDV MGKHKDKMEA
PPCIYPQQIK TLKESFERFY LDKHSGRQLS WQAPMGSADI RAKFVRSNGK VQRYELNVST
YMMVILLLFN DIADGESLTF TQIQEQTQIP ENDLVRNLQS LAVAPKTRVL KKEPMSKDVK
ATDRFSFNHE FQSPFVKVRI GLVAGNANRV ESKDQREETE KKVNEERRHI IEAAVVRIMK
QRKTLTHLNL MNEVLAQLTS RFVPDVKMVK QRIDSLIDRE YLERLGDEAS TYQYLA
//
