ESO1_SCHPO
ID ESO1_SCHPO Reviewed; 872 AA.
AC O42917;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=N-acetyltransferase eso1;
DE EC=2.3.1.-;
DE AltName: Full=ECO1 homolog;
DE AltName: Full=Sister chromatid cohesion protein eso1;
GN Name=eso1; ORFNames=SPBC16A3.11;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10779336; DOI=10.1128/mcb.20.10.3459-3469.2000;
RA Tanaka K., Yonekawa T., Kawasaki Y., Kai M., Furuya K., Iwasaki M.,
RA Murakami H., Yanagida M., Okayama H.;
RT "Fission yeast eso1p is required for establishing sister chromatid cohesion
RT during S phase.";
RL Mol. Cell. Biol. 20:3459-3469(2000).
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 INTERACTION WITH PDS5.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11598020; DOI=10.1093/emboj/20.20.5779;
RA Tanaka K., Hao Z., Kai M., Okayama H.;
RT "Establishment and maintenance of sister chromatid cohesion in fission
RT yeast by a unique mechanism.";
RL EMBO J. 20:5779-5790(2001).
CC -!- FUNCTION: Probable acetyltransferase required for the establishment of
CC sister chromatid cohesion and couple the processes of cohesion and DNA
CC replication to ensure that only sister chromatids become paired
CC together. In contrast to the structural cohesins, the deposition and
CC establishment factors are required only during S phase. The relevance
CC of acetyltransferase function remains unclear (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with pds5. {ECO:0000269|PubMed:11598020}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the acetyltransferase
CC family. ECO subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DNA polymerase
CC type-Y family. {ECO:0000305}.
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DR EMBL; AB039861; BAA95122.1; -; mRNA.
DR EMBL; CU329671; CAA16862.1; -; Genomic_DNA.
DR PIR; T39541; T39541.
DR RefSeq; NP_596778.1; NM_001023799.2.
DR AlphaFoldDB; O42917; -.
DR SMR; O42917; -.
DR BioGRID; 276221; 253.
DR IntAct; O42917; 2.
DR STRING; 4896.SPBC16A3.11.1; -.
DR iPTMnet; O42917; -.
DR MaxQB; O42917; -.
DR PaxDb; O42917; -.
DR EnsemblFungi; SPBC16A3.11.1; SPBC16A3.11.1:pep; SPBC16A3.11.
DR GeneID; 2539666; -.
DR KEGG; spo:SPBC16A3.11; -.
DR PomBase; SPBC16A3.11; eso1.
DR VEuPathDB; FungiDB:SPBC16A3.11; -.
DR eggNOG; KOG2095; Eukaryota.
DR eggNOG; KOG3014; Eukaryota.
DR HOGENOM; CLU_331802_0_0_1; -.
DR InParanoid; O42917; -.
DR OMA; WKKPNNQ; -.
DR PhylomeDB; O42917; -.
DR Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR PRO; PR:O42917; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; IMP:PomBase.
DR GO; GO:0070987; P:error-free translesion synthesis; IMP:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IMP:PomBase.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:PomBase.
DR GO; GO:0061780; P:mitotic cohesin loading; IMP:PomBase.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:PomBase.
DR GO; GO:0009314; P:response to radiation; IBA:GO_Central.
DR GO; GO:0019985; P:translesion synthesis; IMP:PomBase.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041298; UBZ3.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR Pfam; PF18439; zf_UBZ; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51907; ZF_UBZ3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell cycle; DNA damage; DNA repair; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..872
FT /note="N-acetyltransferase eso1"
FT /id="PRO_0000173994"
FT DOMAIN 29..285
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT ZN_FING 533..567
FT /note="UBZ3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT ZN_FING 653..677
FT /note="CCHH-type"
FT REGION 1..591
FT /note="Polymerase type-Y"
FT REGION 569..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..872
FT /note="Acetyltransferase"
FT COMPBIAS 572..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
SQ SEQUENCE 872 AA; 98909 MW; 36ECCD2BC0AEFE94 CRC64;
MELGKSKFSW KDLQYCDKAG TQNSPLRVVA HIDQDAFYAQ VESVRLGLDH SVPLAVQQWQ
GLIAVNYAAR AANISRHETV TEAKKKCPEL CTAHVKTWKA GESEAKYHEN PNPNYYKTCL
DPYRHESVKI LNIIKKHAPV VKKASIDECF IELTSDVKRI VLEEYPYLKI PSEDSNVALP
QAPVLLWPAE FGMVIEEEVV DRTKEDYERD WDDVFLFYAA KIVKEIRDDI YLQLKYTCSA
GVSFNPMLSK LVSSRNKPNK QTILTKNAIQ DYLVSLKITD IRMLGGKFGE EIINLLGTDS
IKDVWNMSMD FLIDKLGQTN GPLVWNLCHG IDNTEITTQV QIKSMLSAKN FSQQKVKSEE
DAINWFQVFA SDLRSRFLEL EGMRRPKTIC LTVVSRFLRK SRSSQIPMNV DISTQFIVEA
TSKLLRQLQQ EFDVYPISNL SISFQNIIEV DRNSRGIEGF LKKSNDEIYM STSVSPSIEG
RAKLLNENMR ENNSFELSSE KDIKSPKRLK RGKGKGIFDM LQQTAVSKPT ENSADETYTC
EECEQKITLS ERNEHEDYHI ALSISRKERY NNLVPPSHDK PKQVKPKTYG RKTGSKHYAP
LSDETNNKRA FLDAFLGNGG NLTPNWKKQT PKAISNSSDN MTQLHLDLAN STVTCSECSM
EYNSTSEEDI LLHSRFHSRV LGGVTVSFQC SPIYRVNYGL SSDCIYSINS ESSLIDQRKA
EEALSFVNNE LSSEPIETIG VDKYTTFLFI SDKKCVGLLL AERISSAYIV DELELNNNNS
TSSAVYIKNE NLRKGFVLGI SRIWVSASRR KQGIASLLLD NALKKFIYGY VISPAEVAFS
QPSESGKQFI ISWHRSRNNG SSKSLRYAVY ES
