DMA2_YEAS7
ID DMA2_YEAS7 Reviewed; 522 AA.
AC A6ZRW7; B0KZW4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=E3 ubiquitin-protein ligase DMA2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P53924};
DE AltName: Full=Checkpoint forkhead associated with RING domains-containing protein 1;
DE AltName: Full=Defective in mitotic arrest protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase DMA2 {ECO:0000305};
GN Name=DMA2; Synonyms=CHF2; ORFNames=SCY_4678;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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. Involved in nutritional control of the
CC cell cycle. Required for proper spindle positioning, likely regulating
CC septin ring deposition at the bud neck. {ECO:0000250|UniProtKB:P53924}.
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:0000250|UniProtKB:P53924};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: UBC4-dependent autoubiquitination occurs at Lys-211, Lys-258, Lys-
CC 288, Lys-310, Lys-333, Lys-343, Lys-346, Lys-366, Lys-406, Lys-412 and
CC Lys-423. UBC13/MMS2-dependent autoubiquitination occurs at Lys-258,
CC Lys-310, Lys-346 and Lys-366. Lys-211, Lys-256, Lys-288, Lys-310, Lys-
CC 343, Lys-258, Lys-366 and Lys-412 are also ubiquitinated in trans by
CC DMA1 E3 ligase in association with UBC4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DMA1 family. {ECO:0000305}.
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DR EMBL; EF125227; ABN58640.1; -; Genomic_DNA.
DR EMBL; AAFW02000067; EDN62699.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRW7; -.
DR SMR; A6ZRW7; -.
DR PRIDE; A6ZRW7; -.
DR EnsemblFungi; EDN62699; EDN62699; SCY_4678.
DR HOGENOM; CLU_017542_2_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR CDD; cd16458; RING-H2_Dmap_like; 1.
DR Gene3D; 3.30.40.10; -; 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 Pfam; PF00498; FHA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Metal-binding;
KW Mitosis; Phosphoprotein; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..522
FT /note="E3 ubiquitin-protein ligase DMA2"
FT /id="PRO_0000389561"
FT DOMAIN 295..358
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 433..477
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
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"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
FT CROSSLNK 423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53924"
SQ SEQUENCE 522 AA; 57570 MW; BDA3E955BCB208E8 CRC64;
MYTPIPANTP APTAPTSSMT SNSSSASNAN TTSSSGINPR NRASGTPSNE RARPASGISS
FLNTFGIRQN SQTASSSAAP DQRLFGTTPS NSHMSVAMES IDTAPQQQEP RLHHPIQMPL
SAQFHVHRNY QLPISISLTA PTTTDHQQSS AHNFEGNNVG NVQESLNQRQ PNGTNNTTTS
IISMAPAATT RNIVGGADGS TIVNNSQEMY 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
