ID A0A2K3QCL2_9HYPO Unreviewed; 528 AA.
AC A0A2K3QCL2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Protein mlo2 {ECO:0000313|EMBL:PNY25267.1};
GN ORFNames=TCAP_04795 {ECO:0000313|EMBL:PNY25267.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY25267.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY25267.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY25267.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PNY25267.1}.
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; NRSZ01000785; PNY25267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QCL2; -.
DR STRING; 45235.A0A2K3QCL2; -.
DR OrthoDB; 11436at2759; -.
DR Proteomes; UP000236621; 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:UP000236621};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..136
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 64..136
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 57321 MW; C5CEAF2E77F2931A CRC64;
MSTDPPPPAA ASADAIGEAA APGRNDNFSQ QSHASGDSQT AAEFIRSQEL LEADAREALP
YSIESCTKIL GPLRQSVFAC LTCSPPPSKP AGVCYACSVQ CHGEHTLVEI FQKRNFTCDC
GTTRIPSTSP CALRTNEQTN TKGGVHSEEP DANNKYNQNF RNRFCGCECD YDPFQQKGTM
FQCLGLGTQD IGGCGEDWYH PGCLVGMGPQ WFEKMDGHEA KQPNGATNGH ALAAIVEGNE
EQQEGQDTAE QAVDDEDEPP MPPGFPEEDD FEGFLCHKCV EANPWIKRYA GTSGFLPAVF
LEQAESAPKP KADETTSKKR KADDDVEEEA EAKRVKNESE STATDATGDA QPTPAEAPAE
EKRTTDGAAG CKLPNLPPAP TGRFSLFFKE DFREKLCRCS DCYQQMIPHP QLLEEEDVYE
PPVSEDDASQ NGGSTHGSGS LLERGESALR NVDRVRAIEG VMAYNHLKER LKPFFQQFAE
SGQAVGAEDI KAYFAKLRGD EQGIKEAGQA AASSKDEDGD SRREQGGY
//
