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Database: UniProt
Entry: A0A0D1DYR0_USTMA
LinkDB: A0A0D1DYR0_USTMA
Original site: A0A0D1DYR0_USTMA 
ID   A0A0D1DYR0_USTMA        Unreviewed;       986 AA.
AC   A0A0D1DYR0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Component of the spindle assembly checkpoint dma1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UMAG_10658 {ECO:0000313|EMBL:KIS68776.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS68776.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS68776.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM003147; KIS68776.1; -; Genomic_DNA.
DR   RefSeq; XP_011389809.1; XM_011391507.1.
DR   AlphaFoldDB; A0A0D1DYR0; -.
DR   STRING; 237631.A0A0D1DYR0; -.
DR   EnsemblFungi; KIS68776; KIS68776; UMAG_10658.
DR   GeneID; 23566658; -.
DR   KEGG; uma:UMAG_10658; -.
DR   VEuPathDB; FungiDB:UMAG_10658; -.
DR   eggNOG; KOG3872; Eukaryota.
DR   InParanoid; A0A0D1DYR0; -.
DR   OrthoDB; 463769at2759; -.
DR   Proteomes; UP000000561; Chromosome 8.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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   SMART; SM00184; RING; 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   Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          273..320
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          415..459
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..972
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  102401 MW;  035FA795DA9840ED CRC64;
     MSTTNTTGAA ASGSAIGRMF RRYSQNGNSR AESQRPSTRE RDSFNMPRNT SSPALDRDTN
     SPVRVSLSTN NPSAPSPSIA RSASHTANLS TPLSTDTPAA IVASRTLPHI SSASSATSPV
     SYPSVTAATT SASLLQDANS SSRNVQTLPD ASYTDPAATA TASAASGTPS TTRPLNAMHR
     IRLVPHLEAT RSLHFEPIER DLKEGESAVK VGRFTDRQPS HRDPVLAALT GVVNQATMSG
     DVGSSAAPLQ SSRGQPGARG GAIPISGSHG GGGRIDSSRI AFKSKVVSRG HAEIWCEPGG
     KFFIRDTKSS SGTFLNHIRL SGPNLESKPF AIKDGDVVQL GVDYQGGTEE IYRCVKMRVE
     LNRGWQREAN QYNVNAFRQL RALQGNPLSP PNDDKPSGAS AALPTNRQSV SVTDCCICLF
     SVTVCQALFI APCSHVFHYK CIRPLLNLHH PGFSCPLCRT FADLDADVEE DEAWQEALEQ
     EAAAAEARLA QGKQPLEVGT PAVELDAPIA AALPPTLTTA LLNAATTDAP RSSTLVANAA
     IASRPSLGTS ASPLLADLHA GHAGHAAPPR GTAALSRRKN DWARPDTAVG SSAGPLAADE
     TFAAGDAAAD TAGLSAELGE MVVTDRLLNE QATTSANPAS SLHRTVHGAS EMGSPIRRGS
     GPITISGSDR PVHAQRAISA SSALAGPAAL GSPEDGWPSV GAVGGFSPGL DESGTPLNHT
     FLSTLAEAPH VTATNHPSPS SVRDFSPGRS APAQTLVPAI VPAGTSRLRL GENEVNDIHT
     AEAVAGRNKR SSGDGGEDVD TAEEEIGGTT GIGGATFGNL SGASHSKGKA KHDGPSLTFA
     TDVQQQDLVK AGDSSVNLPY KLVGQAPPAS AIVSAKSNGS RAYSRGRSRS RTGRDTMQSD
     SDDQEAAPFQ TYELPPVPRT GPNLNASAYM SYQQHHNTSA HMQHSSADAG RQAGTGNAHG
     ESAPSPTSPA SESKMARFKR RISHAM
//
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