ID   DMA1_YEAST              Reviewed;         416 AA.
AC   P38823; D3DL65; Q66GT1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=E3 ubiquitin-protein ligase DMA1 {ECO:0000305|PubMed:18202552};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:18202552, ECO:0000269|PubMed:23264631};
DE   AltName: Full=Checkpoint forkhead associated with RING domains-containing protein 1 {ECO:0000303|PubMed:15319434};
DE   AltName: Full=Defective in mitotic arrest protein 1 {ECO:0000303|PubMed:15146058};
DE   AltName: Full=RING-type E3 ubiquitin transferase DMA1 {ECO:0000305};
GN   Name=DMA1 {ECO:0000303|PubMed:15146058};
GN   Synonyms=CHF1 {ECO:0000303|PubMed:15319434};
GN   OrderedLocusNames=YHR115C {ECO:0000312|SGD:S000001157};
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH CDC123, AND
RP   MUTAGENESIS OF GLY-192; SER-220; HIS-223; CYS-345 AND HIS-350.
RX   PubMed=15319434; DOI=10.1074/jbc.m406151200;
RA   Bieganowski P., Shilinski K., Tsichlis P.N., Brenner C.;
RT   "Cdc123 and checkpoint forkhead associated with RING proteins control the
RT   cell cycle by controlling eIF2gamma abundance.";
RL   J. Biol. Chem. 279:44656-44666(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=15146058; DOI=10.1091/mbc.e04-02-0094;
RA   Fraschini R., Bilotta D., Lucchini G., Piatti S.;
RT   "Functional characterization of Dma1 and Dma2, the budding yeast homologues
RT   of Schizosaccharomyces pombe Dma1 and human Chfr.";
RL   Mol. Biol. Cell 15:3796-3810(2004).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   UBIQUITINATION AT LYS-150; LYS-204; LYS-217; LYS-237; LYS-240; LYS-260;
RP   LYS-300; LYS-306; LYS-313 AND LYS-317.
RX   PubMed=18202552; DOI=10.4161/cc.7.1.5113;
RA   Loring G.L., Christensen K.C., Gerber S.A., Brenner C.;
RT   "Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and
RT   Ubc13/Mms2-dependent ubiquitination.";
RL   Cell Cycle 7:96-105(2008).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND INTERACTION WITH PCL1.
RX   PubMed=23264631; DOI=10.1074/jbc.m112.426593;
RA   Hernandez-Ortega S., Bru S., Ricco N., Ramirez S., Casals N., Jimenez J.,
RA   Isasa M., Crosas B., Clotet J.;
RT   "Defective in mitotic arrest 1 (Dma1) ubiquitin ligase controls G1 cyclin
RT   degradation.";
RL   J. Biol. Chem. 288:4704-4714(2013).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which functions in cell cycle
CC       retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2
CC       ubiquitin conjugating enzymes (PubMed:18202552). Involved in
CC       nutritional control of the cell cycle (PubMed:15319434). Targets the G1
CC       cyclin PCL1 for destruction (PubMed:23264631). Required for proper
CC       spindle positioning, likely regulating septin ring deposition at the
CC       bud neck (PubMed:15146058). {ECO:0000269|PubMed:15146058,
CC       ECO:0000269|PubMed:15319434, ECO:0000269|PubMed:18202552,
CC       ECO:0000269|PubMed:23264631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18202552,
CC         ECO:0000269|PubMed:23264631};
CC   -!- SUBUNIT: Interacts with CDC123 (PubMed:15319434). Interacts with PCL1
CC       (PubMed:23264631). {ECO:0000269|PubMed:15319434,
CC       ECO:0000269|PubMed:23264631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Protein levels are regulated by nutrient status, being high
CC       under good nutrient conditions. {ECO:0000269|PubMed:23264631}.
CC   -!- PTM: UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-
CC       217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317.
CC       UBC4-dependent autoubiquitination is responsible for DMA2 turnover.
CC       UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306.
CC       Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase
CC       in association with UBC4. {ECO:0000269|PubMed:18202552}.
CC   -!- MISCELLANEOUS: Present with 2790 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DMA1 family. {ECO:0000305}.
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DR   EMBL; BK005578; DAA05593.1; -; Genomic_DNA.
DR   EMBL; U00059; AAB68865.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06809.1; -; Genomic_DNA.
DR   PIR; S48957; S48957.
DR   RefSeq; NP_011983.1; NM_001179245.1.
DR   AlphaFoldDB; P38823; -.
DR   SMR; P38823; -.
DR   BioGRID; 36548; 93.
DR   DIP; DIP-1884N; -.
DR   IntAct; P38823; 24.
DR   MINT; P38823; -.
DR   STRING; 4932.YHR115C; -.
DR   iPTMnet; P38823; -.
DR   MaxQB; P38823; -.
DR   PaxDb; 4932-YHR115C; -.
DR   PeptideAtlas; P38823; -.
DR   EnsemblFungi; YHR115C_mRNA; YHR115C; YHR115C.
DR   GeneID; 856515; -.
DR   KEGG; sce:YHR115C; -.
DR   AGR; SGD:S000001157; -.
DR   SGD; S000001157; DMA1.
DR   VEuPathDB; FungiDB:YHR115C; -.
DR   eggNOG; KOG3872; Eukaryota.
DR   GeneTree; ENSGT00940000176812; -.
DR   HOGENOM; CLU_017542_2_0_1; -.
DR   InParanoid; P38823; -.
DR   OMA; SHSWHYQ; -.
DR   OrthoDB; 463769at2759; -.
DR   BioCyc; YEAST:G3O-31157-MONOMER; -.
DR   BioGRID-ORCS; 856515; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38823; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38823; Protein.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR   GO; GO:0032186; P:cellular bud neck septin ring organization; IGI:SGD.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:SGD.
DR   GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:SGD.
DR   GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR   GO; GO:0090337; P:regulation of formin-nucleated actin cable assembly; IMP:SGD.
DR   GO; GO:0000921; P:septin ring assembly; IGI:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:SGD.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Metal-binding;
KW   Mitosis; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..416
FT                   /note="E3 ubiquitin-protein ligase DMA1"
FT                   /id="PRO_0000056338"
FT   DOMAIN          189..252
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   ZN_FING         327..371
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        150
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        204
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        217
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        237
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        300
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        306
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        313
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18202552"
FT   MUTAGEN         192
FT                   /note="G->E: Decreases the interaction with CDC123."
FT                   /evidence="ECO:0000269|PubMed:15319434"
FT   MUTAGEN         220
FT                   /note="S->A: Decreases the interaction with CDC123, when
FT                   associated with L-223."
FT                   /evidence="ECO:0000269|PubMed:15319434"
FT   MUTAGEN         223
FT                   /note="H->L: Decreases the interaction with CDC123, when
FT                   associated with A-220."
FT                   /evidence="ECO:0000269|PubMed:15319434"
FT   MUTAGEN         345
FT                   /note="C->S: Decreases the interaction with CDC123, when
FT                   associated with A-350."
FT                   /evidence="ECO:0000269|PubMed:15319434"
FT   MUTAGEN         350
FT                   /note="H->A: Decreases the interaction with CDC123, when
FT                   associated with S-345."
FT                   /evidence="ECO:0000269|PubMed:15319434"
SQ   SEQUENCE   416 AA;  46098 MW;  4344AB155C83CBF7 CRC64;
     MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN NSNNNSVSNG
     LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP AVNTTKSIRH FIYPPNQVNQ
     TEFSLDIHLP PNTSLPERID QSTLKRRMDK HGLFSIRLTP FIDTSSTSVA NQGLFFDPII
     RTAGAGSQII IGRYTERVRE AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK
     SSSGTFLNHQ RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK
     ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH FHCVRRLVIM
     NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM DIDMEINNNL GVRLVD
//