DMA1_SCHPO
ID DMA1_SCHPO Reviewed; 267 AA.
AC Q10322;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable E3 ubiquitin-protein ligase dma1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P38823};
DE AltName: Full=RING-type E3 ubiquitin transferase dma1 {ECO:0000305};
GN Name=dma1; ORFNames=SPAC17G8.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8978687; DOI=10.1002/j.1460-2075.1996.tb01051.x;
RA Murone M., Simanis V.;
RT "The fission yeast dma1 gene is a component of the spindle assembly
RT checkpoint, required to prevent septum formation and premature exit from
RT mitosis if spindle function is compromised.";
RL EMBO J. 15:6605-6616(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, INTERACTION WITH SID4, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF ARG-64; HIS-88; CYS-210 AND HIS-212.
RX PubMed=12479804; DOI=10.1016/s1534-5807(02)00367-2;
RA Guertin D.A., Venkatram S., Gould K.L., McCollum D.;
RT "Dma1 prevents mitotic exit and cytokinesis by inhibiting the septation
RT initiation network (SIN).";
RL Dev. Cell 3:779-790(2002).
RN [4]
RP INTERACTION WITH SID4.
RX PubMed=15062098; DOI=10.1016/j.cub.2004.03.036;
RA Morrell J.L., Tomlin G.C., Rajagopalan S., Venkatram S., Feoktistova A.S.,
RA Tasto J.J., Mehta S., Jennings J.L., Link A., Balasubramanian M.K.,
RA Gould K.L.;
RT "Sid4p-Cdc11p assembles the septation initiation network and its regulators
RT at the S. pombe SPB.";
RL Curr. Biol. 14:579-584(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which is a component of
CC the spindle assembly checkpoint, required to prevent septum formation
CC and premature exit from mitosis if spindle function is compromised.
CC Inhibits the septation initiation netwok (SIN) during spindle
CC checkpoint activation. The effect appears to be mediated through
CC preventing the SIN activator, plo1 kinase, from localizing to the SPB.
CC {ECO:0000269|PubMed:12479804, ECO:0000269|PubMed:8978687}.
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:P38823};
CC -!- SUBUNIT: Interacts with sid4. {ECO:0000269|PubMed:12479804,
CC ECO:0000269|PubMed:15062098}.
CC -!- INTERACTION:
CC Q10322; O60187: sid4; NbExp=2; IntAct=EBI-1125055, EBI-1125100;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:12479804,
CC ECO:0000269|PubMed:16823372}. Note=Localizes also at the division site
CC in mitosis.
CC -!- DOMAIN: The FHA domain is required for the proper localization at the
CC SPB. {ECO:0000269|PubMed:12479804}.
CC -!- SIMILARITY: Belongs to the DMA1 family. {ECO:0000305}.
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DR EMBL; X81883; CAA57466.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93693.1; -; Genomic_DNA.
DR PIR; T37862; T37862.
DR RefSeq; NP_593733.1; NM_001019164.2.
DR AlphaFoldDB; Q10322; -.
DR SMR; Q10322; -.
DR BioGRID; 278873; 51.
DR IntAct; Q10322; 10.
DR STRING; 4896.SPAC17G8.10c.1; -.
DR iPTMnet; Q10322; -.
DR MaxQB; Q10322; -.
DR PaxDb; Q10322; -.
DR EnsemblFungi; SPAC17G8.10c.1; SPAC17G8.10c.1:pep; SPAC17G8.10c.
DR GeneID; 2542409; -.
DR KEGG; spo:SPAC17G8.10c; -.
DR PomBase; SPAC17G8.10c; dma1.
DR VEuPathDB; FungiDB:SPAC17G8.10c; -.
DR eggNOG; KOG3872; Eukaryota.
DR HOGENOM; CLU_026302_0_0_1; -.
DR InParanoid; Q10322; -.
DR OMA; FICRKYH; -.
DR PhylomeDB; Q10322; -.
DR PRO; PR:Q10322; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
DR GO; GO:1903024; P:positive regulation of ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0043938; P:positive regulation of sporulation; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
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; cd00060; FHA; 1.
DR Gene3D; 3.30.40.10; -; 1.
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 SMART; SM00184; RING; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="Probable E3 ubiquitin-protein ligase dma1"
FT /id="PRO_0000055897"
FT DOMAIN 60..116
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 192..236
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 64
FT /note="R->A: Impairs dma1 proper localization and ability
FT to maintain spindle checkpoint arrest."
FT /evidence="ECO:0000269|PubMed:12479804"
FT MUTAGEN 88
FT /note="H->A: Impairs dma1 proper localization and ability
FT to maintain spindle checkpoint arrest."
FT /evidence="ECO:0000269|PubMed:12479804"
FT MUTAGEN 210
FT /note="C->A: Impairs ability to maintain spindle checkpoint
FT arrest; when associated with A-210."
FT /evidence="ECO:0000269|PubMed:12479804"
FT MUTAGEN 212
FT /note="H->A: Impairs ability to maintain spindle checkpoint
FT arrest; when associated with A-212."
FT /evidence="ECO:0000269|PubMed:12479804"
SQ SEQUENCE 267 AA; 30597 MW; 35CA43E6E30B4B8A CRC64;
MTKSVEGYLK EQELAAETDS EKDDDKISIR LTNFVGPNAH SFSFDPLVRY WNRKQNNLPI
YIGRYTERYN GGDVSAIVFR SKVVSRRHAQ IFYENNTWYI QDMGSSSGTF LNHVRLSPPS
KTSKPYPISN NDILQLGADY RGGHEVNYRC VRARVELNNS WKIKLSPYNL NEFKRMQELV
LCGSSESGPP ECCICLMPVL PCQALFVAPC SHSYHYKCIR PTLNESHPYF SCFICRKYHD
LEAPVEEGDE SLNDLLRNAT VKDDASE
