ID   ABP1_SCHPO              Reviewed;         522 AA.
AC   P49777; Q9URU7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   14-DEC-2011, entry version 93.
DE   RecName: Full=ARS-binding protein 1;
GN   Name=abp1; ORFNames=SPBC1105.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   MEDLINE=96133965; PubMed=8552670; DOI=10.1073/pnas.93.1.502;
RA   Murakami Y., Huberman J.A., Hurwitz J.;
RT   "Identification, purification, and molecular cloning of autonomously
RT   replicating sequence-binding protein 1 from fission yeast
RT   Schizosaccharomyces pombe.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:502-507(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
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 ABP1.
RX   PubMed=17112379; DOI=10.1186/1747-1028-1-27;
RA   Locovei A.M., Spiga M.-G., Tanaka K., Murakami Y., D'Urso G.;
RT   "The CENP-B homolog, Abp1, interacts with the initiation protein Cdc23
RT   (MCM10) and is required for efficient DNA replication in fission
RT   yeast.";
RL   Cell Div. 1:27-27(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Binds, preferentially, to the Maundrell ARS consensus
CC       sequence within ARS3002.
CC   -!- SUBUNIT: Interacts with mcm10.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 1 HTH CENPB-type DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U39079; AAB01537.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB50967.1; -; Genomic_DNA.
DR   PIR; T39281; T39281.
DR   RefSeq; NP_596460.1; NM_001022379.1.
DR   PDB; 1IUF; NMR; -; A=1-141.
DR   PDBsum; 1IUF; -.
DR   ProteinModelPortal; P49777; -.
DR   SMR; P49777; 1-141.
DR   IntAct; P49777; 2.
DR   STRING; P49777; -.
DR   EnsemblFungi; SPBC1105.04c.1; SPBC1105.04c.1:pep; SPBC1105.04c.
DR   GeneID; 2539971; -.
DR   GenomeReviews; CU329671_GR; abp1.
DR   KEGG; spo:SPBC1105.04c; -.
DR   NMPDR; fig|4896.1.peg.2326; -.
DR   GeneDB_Spombe; SPBC1105.04c; -.
DR   eggNOG; fuNOG05144; -.
DR   GeneTree; EFGT00050000007452; -.
DR   HOGENOM; HBG207912; -.
DR   OMA; ANTHARM; -.
DR   OrthoDB; EOG4DRDN0; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004461-MONOMER; -.
DR   ArrayExpress; P49777; -.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:GeneDB_Spombe.
DR   GO; GO:0000790; C:nuclear chromatin; IC:GeneDB_Spombe.
DR   GO; GO:0019237; F:centromeric DNA binding; IDA:GeneDB_Spombe.
DR   GO; GO:0046983; F:protein dimerization activity; NAS:GeneDB_Spombe.
DR   GO; GO:0030702; P:chromatin silencing at centromere; IMP:GeneDB_Spombe.
DR   GO; GO:0006270; P:DNA-dependent DNA replication initiation; IMP:GeneDB_Spombe.
DR   GO; GO:0016570; P:histone modification; IMP:GeneDB_Spombe.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:GeneDB_Spombe.
DR   InterPro; IPR004875; DDE_SF_endonuclease_CENPB-like.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR006600; Pogo/CenpB/PDC2_DNA-bd_HTH.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 2.
DR   Pfam; PF03184; DDE_1; 1.
DR   Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR   SMART; SM00674; CENPB; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51253; HTH_CENPB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    522       ARS-binding protein 1.
FT                                /FTId=PRO_0000126133.
FT   DOMAIN       70    144       HTH CENPB-type.
FT   MOD_RES     460    460       Phosphothreonine.
FT   CONFLICT    336    336       C -> S (in Ref. 1; AAB01537).
FT   STRAND        5      7
FT   HELIX        12     22
FT   STRAND       23     26
FT   HELIX        30     41
FT   STRAND       46     49
FT   HELIX        52     60
FT   TURN         61     63
FT   STRAND       66     72
FT   HELIX        80     92
FT   HELIX       102    114
FT   STRAND      116    119
FT   HELIX       129    137
SQ   SEQUENCE   522 AA;  59840 MW;  8D50078EA9E2233F CRC64;
     MGKIKRRAIT EHEKRALRHY FFQLQNRSGQ QDLIEWFREK FGKDISQPSV SQILSSKYSY
     LDNTVEKPWD VKRNRPPKYP LLEAALFEWQ VQQGDDATLS GETIKRAAAI LWHKIPEYQD
     QPVPNFSNGW LEGFRKRHIL HAINEQPTES VVLNNTEPPN DPLSRVYDVT RLTNINDIFT
     MQETGLFWKL VPNGTPEVED IKGITRFKAR ITLTVCCNAS GTERLPLWVI GYSQSPRVFR
     AANVKPEVMN FKWRSNGKAS MTTAIMEEWL RWFDACMEGR KVILLIDSYT PHLRAVENIR
     NSGNDLRNTT VITLPSTSAS ISQPCSEGVI YALKACYRKH WVQYILEQNE LGRNPYNTTN
     VLRAILWLVK AWTTDISPEI IENAFNLSGV LGLFNESAVT SRALDEMIHP LRELVSEFSV
     QAAMRIEDFI SPSEENIVDS SEDIINQIAS QYMDDRAFET DEEESTEFQI TTKDAMKAIE
     LLLNYEAQQP DGNPAITISL LNYQKLLEAR GGNVNLSRLR ST
//