ID K1XWK2_MARBU Unreviewed; 547 AA.
AC K1XWK2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Metaphase-anaphase transition protein {ECO:0000313|EMBL:EKD17114.1};
GN ORFNames=MBM_04691 {ECO:0000313|EMBL:EKD17114.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17114.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD17114.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17114.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921437; EKD17114.1; -; Genomic_DNA.
DR RefSeq; XP_007292580.1; XM_007292518.1.
DR AlphaFoldDB; K1XWK2; -.
DR STRING; 1072389.K1XWK2; -.
DR GeneID; 18760626; -.
DR KEGG; mbe:MBM_04691; -.
DR eggNOG; KOG2752; Eukaryota.
DR HOGENOM; CLU_025221_1_0_1; -.
DR InParanoid; K1XWK2; -.
DR OMA; GAMVYNH; -.
DR OrthoDB; 11436at2759; -.
DR Proteomes; UP000006753; 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:UP000006753};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..142
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 64..142
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 59136 MW; C226FF6F681B204D CRC64;
MDAPPTTDSS FSEQPNSSAS GPSRTQSFSQ QTDSSQTSQT AAEFIDRQLQ LEAEAREALP
YKFEKCTQPI GKLRQQIFSC LTCNPPPANP TDPYTAAGVC YSCSISCHGE HTLVELFNKR
DFVCDCGTTR LPATSHCSLR INPETNTKGG IHSEEPAPEN TYNHNFRNRF CGCGCDYDAY
AQKGTMFQCL GIGTGETGGC GEDWWHPGCL VGLGPDWDES SGRKPKNEGF LESIVEVAEA
VVDEKEGEAK AATTNGDASK VPADVIPEVE DEDEDPPLPP GFPEEDDFEG FLCYKCVEAN
PWIKFYAGTP GFLPPVFRRS TAPSPETGIV AKTEELITSV LPTNKKRKAD DDGESSSSKR
VKDEGPTASS EPSTTDTPAT TVDPIQTEEG KPPCKLTTLP PPPTGVFSLF FTPDFRTHLC
RCPSCFPLLT PHPQLLEEEE LYEPSVSSSE DGAGGGSTVG SGSIYDLGES ALKNVDRVRA
IEGVMAYNHL KDKLKPFFQQ FAESGQAISA EDIKAHFAKM RGDAEAIRDA GQEAQVAGDS
RKEQGGF
//
