ABP1_SCHPO
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 03-AUG-2022, entry version 156.
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; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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 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 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 yeast.";
RL Cell Div. 1:27-27(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND IDENTIFICATION BY
RP MASS 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. {ECO:0000269|PubMed:17112379}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; U39079; AAB01537.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB50967.1; -; Genomic_DNA.
DR PIR; T39281; T39281.
DR RefSeq; NP_596460.1; NM_001022379.2.
DR PDB; 1IUF; NMR; -; A=1-141.
DR PDBsum; 1IUF; -.
DR AlphaFoldDB; P49777; -.
DR SMR; P49777; -.
DR BioGRID; 276515; 132.
DR IntAct; P49777; 2.
DR STRING; 4896.SPBC1105.04c.1; -.
DR iPTMnet; P49777; -.
DR MaxQB; P49777; -.
DR PaxDb; P49777; -.
DR PRIDE; P49777; -.
DR EnsemblFungi; SPBC1105.04c.1; SPBC1105.04c.1:pep; SPBC1105.04c.
DR GeneID; 2539971; -.
DR KEGG; spo:SPBC1105.04c; -.
DR PomBase; SPBC1105.04c; -.
DR VEuPathDB; FungiDB:SPBC1105.04c; -.
DR eggNOG; KOG3105; Eukaryota.
DR HOGENOM; CLU_018294_0_3_1; -.
DR InParanoid; P49777; -.
DR OMA; HKASEMP; -.
DR PhylomeDB; P49777; -.
DR EvolutionaryTrace; P49777; -.
DR PRO; PR:P49777; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IC:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0007535; P:donor selection; IMP:PomBase.
DR GO; GO:1903212; P:protein localization to mating-type region heterochromatin; IMP:PomBase.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR041188; HTH_ABP1_N.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF18107; HTH_ABP1_N; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR SMART; SM00674; CENPB; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51253; HTH_CENPB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..522
FT /note="ARS-binding protein 1"
FT /id="PRO_0000126133"
FT DOMAIN 70..144
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 336
FT /note="C -> S (in Ref. 1; AAB01537)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1IUF"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1IUF"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1IUF"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1IUF"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1IUF"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1IUF"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1IUF"
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
