ID H0GM73_SACCK Unreviewed; 522 AA.
AC H0GM73;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dma2p {ECO:0000313|EMBL:EHN05101.1};
GN ORFNames=VIN7_4136 {ECO:0000313|EMBL:EHN05101.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN05101.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN05101.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN05101.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
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:EHN05101.1}.
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DR EMBL; AGVY01000044; EHN05101.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GM73; -.
DR SMR; H0GM73; -.
DR HOGENOM; CLU_017542_2_0_1; -.
DR PhylomeDB; H0GM73; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR CDD; cd22692; FHA_DMA-like; 1.
DR CDD; cd16458; RING-H2_Dmap-like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042823; Dma1/Dma2_RING-H2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 295..358
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 433..477
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57535 MW; FED51620F0C8BEF8 CRC64;
MYTPIPANTP APAAPTSSMT SNSSSASNAN TTSSSGINPR NRASGTPSNE RARPASGISS
FLNTFGIRQN SQTASSSAAP DQRLFGTTPS NSHMSVAMES IDTAPQQQEP HLHHPIQMPL
SAQFHVHRNY QLPISISLTA PTTTDHQQLS AHNFEGNNVG NVQESLNQRQ PNGTNNTTTS
IISMAPAATT RNIVGGADGS TTVNNSQEMY KNLRHLIYAA NQPNGTEILH LDLPATSAEE
SNNMFNVDEV TLKQRKDKHG LFSIRLTPFI DSSSTTNQGL FFEPIIRKAG PGSQLVIGRY
TERVRDAISK IPEQYHPVVF KSKVVSRTHG CFKVDSQGNW YIKDVKSSSG TFLNHQRLSP
ASSLSKDTPL RDGDILQLGM DFRGGTEEIY RCVRMRIELN RSWKLKANSF NKEALQRLQN
LQKLTTGVEE EDCSICLCKI KPCQAIFISP CAHSWHFRCV RRLVMLSYPQ FVCPNCRSSC
DLEASFESSD EEDESDVESE GDQLVDQLSV LMETSKDVDS HP
//
