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Database: UniProt
Entry: A0A1V6R5H3_9EURO
LinkDB: A0A1V6R5H3_9EURO
Original site: A0A1V6R5H3_9EURO 
ID   A0A1V6R5H3_9EURO        Unreviewed;       525 AA.
AC   A0A1V6R5H3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=UBR-type domain-containing protein {ECO:0000259|PROSITE:PS51157};
GN   ORFNames=PENSOL_c015G10943 {ECO:0000313|EMBL:OQD96725.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD96725.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD96725.1}.
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DR   EMBL; MDYO01000015; OQD96725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6R5H3; -.
DR   STRING; 60172.A0A1V6R5H3; -.
DR   OrthoDB; 11436at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19677; UBR-box_UBR7; 1.
DR   InterPro; IPR040204; UBR7.
DR   InterPro; IPR047506; UBR7-like_UBR-box.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR13513; E3 UBIQUITIN-PROTEIN LIGASE UBR7; 1.
DR   PANTHER; PTHR13513:SF9; E3 UBIQUITIN-PROTEIN LIGASE UBR7-RELATED; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          51..129
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         51..129
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  57319 MW;  722D98E71DB22AE2 CRC64;
     MDPTHSVVAQ LAEDARSESM GSQNSQTAKE FIESQLQLEA DAREALPYAF DSCTYDLGPL
     RQVLFACLTC NPPPTDSNES YTAAAVCYSC SIACHGEHTL VELFNKRNFV CDCGTTRLPS
     SSCCTLREDP ATGKKGVHSQ KAAAGNAYNH NFRNQFCGCG EQYDAYSEKG TMYQCLGLGT
     VETGGCGEDW WHPECLIGLS RDWNKAAPKA SGLGGGDATN DVPAEDEEDI LPPGFPAEDD
     FDHLICFKCI DSNPWIKPYA GTPGFLPPVF REGGLKKISN VTEDLSVPDT EPKETEPKET
     EHEEIEPKDQ EKTEHSKKRK ADDEGPIEGE PVTKRTKEEE ASVEEQPSKA VKEEETTKKE
     SDASTKPYPP KHTELPKSTP VESFSLFALE DFHGQLCRCA ECFPKLVPHP QLREEEDTYE
     PPMSDDGQAN GAASVGTGSI YDRGEAALNN MDRVRAIEGA MAYNHLRDKL KVFLQPFAES
     GQAVSAEDIK GYFEALRGDE QGIKDAANHA STVGGDGKDD TSGDK
//
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