ORC4_SCHPO
ID ORC4_SCHPO Reviewed; 972 AA.
AC Q9Y794;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Origin recognition complex subunit 4;
GN Name=orc4; Synonyms=orp4; ORFNames=SPBP23A10.13;
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], AND CHARACTERIZATION.
RX PubMed=10077566; DOI=10.1073/pnas.96.6.2656;
RA Chuang R.-Y., Kelly T.J.;
RT "The fission yeast homologue of Orc4p binds to replication origin DNA via
RT multiple AT-hooks.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2656-2661(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=10535928; DOI=10.1073/pnas.96.22.12367;
RA Moon K.-Y., Kong D., Lee J.-K., Raychaudhuri S., Hurwitz J.;
RT "Identification and reconstitution of the origin recognition complex from
RT Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12367-12372(1999).
RN [3]
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 [4]
RP FUNCTION, CHARACTERIZATION OF ORC, AND INTERACTION WITH CDC18.
RX PubMed=11850415; DOI=10.1074/jbc.m107710200;
RA Chuang R.-Y., Chretien L., Dai J., Kelly T.J.;
RT "Purification and characterization of the Schizosaccharomyces pombe origin
RT recognition complex: interaction with origin DNA and Cdc18 protein.";
RL J. Biol. Chem. 277:16920-16927(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-405; SER-406 AND SER-503, AND
RP IDENTIFICATION BY 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: Component of the origin recognition complex (ORC) that binds
CC origins of replication. It has a role in both chromosomal replication
CC and mating type transcriptional silencing. ORC binds to multiple sites
CC within the ars1 origin of DNA replication in an ATP-independent manner.
CC This binding is mediated by the N-terminal A.T hook repeats of orc4.
CC {ECO:0000269|PubMed:11850415}.
CC -!- SUBUNIT: ORC is composed of six subunits. ORC interacts with cdc18,
CC recruiting it to the ars1 origin of replication.
CC {ECO:0000269|PubMed:10535928, ECO:0000269|PubMed:11850415}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the ORC4 family. {ECO:0000305}.
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DR EMBL; AF125185; AAD21618.1; -; mRNA.
DR EMBL; CU329671; CAB66441.1; -; Genomic_DNA.
DR PIR; T50400; T50400.
DR RefSeq; NP_595825.1; NM_001021729.2.
DR AlphaFoldDB; Q9Y794; -.
DR SMR; Q9Y794; -.
DR BioGRID; 277810; 7.
DR STRING; 4896.SPBP23A10.13.1; -.
DR iPTMnet; Q9Y794; -.
DR MaxQB; Q9Y794; -.
DR PaxDb; Q9Y794; -.
DR PRIDE; Q9Y794; -.
DR EnsemblFungi; SPBP23A10.13.1; SPBP23A10.13.1:pep; SPBP23A10.13.
DR GeneID; 2541298; -.
DR KEGG; spo:SPBP23A10.13; -.
DR PomBase; SPBP23A10.13; orc4.
DR VEuPathDB; FungiDB:SPBP23A10.13; -.
DR eggNOG; KOG2228; Eukaryota.
DR HOGENOM; CLU_322661_0_0_1; -.
DR InParanoid; Q9Y794; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SPO-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q9Y794; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; NAS:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IDA:PomBase.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IC:PomBase.
DR GO; GO:1902597; P:positive regulation of DNA replication origin binding; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR016527; ORC4.
DR InterPro; IPR032705; ORC4_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12087; PTHR12087; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF02178; AT_hook; 8.
DR Pfam; PF14629; ORC4_C; 1.
DR PRINTS; PR00929; ATHOOK.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00384; AT_hook; 9.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..972
FT /note="Origin recognition complex subunit 4"
FT /id="PRO_0000127090"
FT DNA_BIND 100..112
FT /note="A.T hook 1"
FT DNA_BIND 123..135
FT /note="A.T hook 2"
FT DNA_BIND 148..160
FT /note="A.T hook 3"
FT DNA_BIND 201..213
FT /note="A.T hook 4"
FT DNA_BIND 231..243
FT /note="A.T hook 5"
FT DNA_BIND 310..322
FT /note="A.T hook 6"
FT DNA_BIND 339..351
FT /note="A.T hook 7"
FT DNA_BIND 364..376
FT /note="A.T hook 8"
FT DNA_BIND 425..437
FT /note="A.T hook 9"
FT REGION 31..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541..548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 582..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 972 AA; 108613 MW; 412F58A6107D4E58 CRC64;
MSSSPFTNLG NLDTEAIYEN KENEYQTNIT NETSNVQNLS SGNDDQQYPN STNDDANNGL
TASQAKLQDI AAVTLFQDNN ISTTTLAPPS PSPLRLNEAP RRRGRPRKYP PKPIDEGSEP
IIKRKRGRPP KIKSSSPSTK LDDPLKPKRG RGRPRLHPLP VVQPSVDEGT TQNNLQMGLD
EPNIIEGFAE GHANLSELKP KRGRGRPRKI KPEEGSSSQN GLSPLVVLPA KRGRGRPPLH
RSEQKIANTP ISNNVTVEST GTNLHTHSQL NPENEQSSSE FYSLNPQSEI RKEVVVTDQP
LFSTADVPVK RKRGRPPLNK PKILFGTSTE NKIDENRPKR GRGRPRLERP SGLPLDSKSQ
SLFKRKRGRP PKIASGIVPL SAFTRKHEDM LHDSDALSLK HFAITSPNNQ QFLNNQQRES
APLLPRKRGR PPKKRQENAE IRNITPGLTD SSVHSSSATP QSESSSPNSV SPLLPSSDRL
PLLRQSQFTP PPKKPNFEVA IISPKKSQHK LYPNPVVESV FNDVPYSEID SQLHTIKSTI
AARLCGKSHI PLVGHMDEQT KLYQWVRQTI VLGEGNSVII VGPRGSGKSV LVDDILSRAA
QEINEKSYVV RLNGTYQTDD KLALREISRQ LSIELESIES DEALKSEMNF SDTLTKLLAT
LSHPVDLGIA EDVMTTSAAV IFVLEEFDLF VQHSRQMLLY NLFDIAQSRK APILIIGLTT
RYDCSESLEK RVKSRFSHMV IPMRPPSSLS EFEQILKSVL YVSDEGGKDQ IITCWNQRVD
ELLSDTRSHL HKLVQHHYFA SRNLKLLYVD LLFPILSMAP DRPLLADEDF ANISLKVSDH
KVELVKNLSL LELALLICAV RFEARDIPAC NFNSAYQEYR QLHQSSVINA AASGALAHSS
RLWGRDVALE AWETLGSIGL IIPVHPSTNV SGALSRQCQL WQPEVDINVV SVGLREHRRL
PSHYYRWLKE VI
