ID A0A3M2T6A2_9EURO Unreviewed; 521 AA.
AC A0A3M2T6A2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Metaphase-anaphase transition protein {ECO:0000313|EMBL:RMJ25313.1};
GN ORFNames=PHISP_03800 {ECO:0000313|EMBL:RMJ25313.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ25313.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ25313.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ25313.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-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:RMJ25313.1}.
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DR EMBL; RAQS01000126; RMJ25313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2T6A2; -.
DR STRING; 1960876.A0A3M2T6A2; -.
DR Proteomes; UP000272442; 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:UP000272442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 60..138
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 60..138
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 56562 MW; 03CA141AAF1D7FC5 CRC64;
MDNTEPVNPT ASADQQKPEG DQGKRRESFS SQNSQTAKDY INSQLQLEAD AREVLPYAFD
SCTQPLGPLR QSLFACTTCN PPPAGSDDKF TPAAVCYSCS ISCHGEHTLV ELFNRRNFVC
DCGTTRLPSS APCTLRNDPE TGEKGVHSQE PAPDNAYNHN FQNKFCGCGE VYDAYKEKGT
MFQCLGLGTV ETGGCGEDWW HPECLISLPR DWNKTETAGK EKKGEDGTKE EHASAGGDGE
ETPLPPNFPG EDDFDTFICF KCIDSNPWLK RYAGTPGFLP PVYKHGGLAE ASDNKPRQTP
ENSEGQQDGT KKRKADDNSG EEVPAPKRAK EGENSESTDA KAKPEGIDAK QPTHKHESLP
VSAPSGSFSL FLKEDFRDHF CRCPGCYPNL AHHSQLREEE EAYEPPLSDD GETNGGGSAG
TSLLDRGEAA FSTMDRVRAI EGAMVYNRLR DNLKGFLKPY AETGKAVSAE DIKGYFETLR
GDDQAIKDAA GQASAASNGD GNGDDGDGDG DGDNRREQNG Y
//
