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Description:
N-acetyltransferase eso1 (EC 2.3.1.-) (Sister chromatid cohesionprotein eso1) (ECO1 homolog).
Molecular weight: 98909
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
07-MAR-2006, entry version 40.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein ESO1_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AB039861 | BAA95122.1 | - |
| EMBL | AL021748 | CAA16862.1 | - |
| PIR | T39541 | T39541. | |
| HSSP | Q04049 | 1JIH | |
| GeneDB_Spombe | SPBC16A3.11 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-004761-MONOMER | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006260 | P:DNA replication | IMP. |
| GO | GO:0007062 | P:sister chromatid cohesion | IMP. |
| InterPro | IPR002197 | HTH_Fis. | |
| InterPro | IPR001126 | UMUC_like. | |
| Pfam | PF00817 | IMS | 1. |
| PRINTS | PR01590 | HTHFIS. | |
| PROSITE | PS50173 | UMUC | 1. |
Keywords:
Acyltransferase; Cell cycle; Complete proteome; Metal-binding; Nuclear protein; Transferase; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972;
RX MEDLINE=20242040; PubMed=10779336;
RX 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
RT cohesion during S phase.";
RL Mol. Cell. Biol. 20:3459-3469(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; 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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH PDS5.
RC STRAIN=972;
RX MEDLINE=21481773; 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).
Feature:
CHAIN 1 872 N-acetyltransferase eso1.
/FTId=PRO_0000173994.
DOMAIN 29 285 UmuC.
ZN_FING 653 677 CCHH-type.
REGION 1 591 Polymerase type-Y.
REGION 592 872 Acetyltransferase.
Comments:
-!- FUNCTION: Probable acetyltransferase required for the
establishment of sister chromatid cohesion and couple the
processes of cohesion and DNA replication to ensure that only
sister chromatids become paired together. In contrast to the
structural cohesins, the deposition and establishment factors are
required only during S phase. The relevance of acetyltransferase
function remains unclear (By similarity).
-!- SUBUNIT: Interacts with pds5.
-!- SUBCELLULAR LOCATION: Nucleus (Probable).
-!- SIMILARITY: In the C-terminal section; belongs to the
acetyltransferase family. GCN5 subfamily.
-!- SIMILARITY: In the N-terminal section; belongs to the DNA
polymerase type-Y family.
-!- SIMILARITY: Contains 1 umuC domain.
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Sequence length: 872
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