ID   ORC4_YEAST              Reviewed;         529 AA.
AC   P54791; D6W4G3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Origin recognition complex subunit 4;
DE   AltName: Full=Origin recognition complex 56 kDa subunit;
GN   Name=ORC4; OrderedLocusNames=YPR162C; ORFNames=P9325.5;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7585959; DOI=10.1016/0092-8674(95)90096-9;
RA   Bell S.P., Mitchell J., Leber J., Kobayashi R., Stillman B.;
RT   "The multidomain structure of Orc1p reveals similarity to regulators of DNA
RT   replication and transcriptional silencing.";
RL   Cell 83:563-568(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(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. Binds to the ARS consensus
CC       sequence (ACS) of origins of replication.
CC   -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC       at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6.
CC   -!- INTERACTION:
CC       P54791; P54784: ORC1; NbExp=6; IntAct=EBI-12580, EBI-12568;
CC       P54791; P54790: ORC3; NbExp=3; IntAct=EBI-12580, EBI-12576;
CC       P54791; P50874: ORC5; NbExp=9; IntAct=EBI-12580, EBI-12584;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 2170 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ORC4 family. {ECO:0000305}.
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DR   EMBL; U34862; AAB38250.1; -; Genomic_DNA.
DR   EMBL; U25840; AAB68149.1; -; Genomic_DNA.
DR   EMBL; AY723871; AAU09788.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11579.1; -; Genomic_DNA.
DR   PIR; S59821; S59821.
DR   RefSeq; NP_015488.1; NM_001184259.1.
DR   PDB; 5V8F; EM; 3.90 A; D=1-529.
DR   PDB; 5ZR1; EM; 3.00 A; D=1-529.
DR   PDB; 6RQC; EM; 4.40 A; D=1-529.
DR   PDB; 6WGC; EM; 4.30 A; D=1-529.
DR   PDB; 6WGG; EM; 8.10 A; D=1-529.
DR   PDB; 6WGI; EM; 10.00 A; D=1-529.
DR   PDB; 7MCA; EM; 3.60 A; D=1-529.
DR   PDB; 7TJF; EM; 2.60 A; D=1-529.
DR   PDB; 7TJH; EM; 2.50 A; D=1-529.
DR   PDB; 7TJI; EM; 2.70 A; D=1-529.
DR   PDB; 7TJJ; EM; 2.70 A; D=1-529.
DR   PDB; 7TJK; EM; 2.70 A; D=1-529.
DR   PDBsum; 5V8F; -.
DR   PDBsum; 5ZR1; -.
DR   PDBsum; 6RQC; -.
DR   PDBsum; 6WGC; -.
DR   PDBsum; 6WGG; -.
DR   PDBsum; 6WGI; -.
DR   PDBsum; 7MCA; -.
DR   PDBsum; 7TJF; -.
DR   PDBsum; 7TJH; -.
DR   PDBsum; 7TJI; -.
DR   PDBsum; 7TJJ; -.
DR   PDBsum; 7TJK; -.
DR   AlphaFoldDB; P54791; -.
DR   EMDB; EMD-21662; -.
DR   EMDB; EMD-21665; -.
DR   EMDB; EMD-21666; -.
DR   EMDB; EMD-23755; -.
DR   EMDB; EMD-23818; -.
DR   EMDB; EMD-25925; -.
DR   EMDB; EMD-25926; -.
DR   EMDB; EMD-25927; -.
DR   EMDB; EMD-25928; -.
DR   EMDB; EMD-4980; -.
DR   EMDB; EMD-6941; -.
DR   EMDB; EMD-8540; -.
DR   SMR; P54791; -.
DR   BioGRID; 36335; 339.
DR   ComplexPortal; CPX-768; Nuclear origin recognition complex.
DR   DIP; DIP-2287N; -.
DR   IntAct; P54791; 17.
DR   MINT; P54791; -.
DR   STRING; 4932.YPR162C; -.
DR   iPTMnet; P54791; -.
DR   MaxQB; P54791; -.
DR   PaxDb; 4932-YPR162C; -.
DR   PeptideAtlas; P54791; -.
DR   EnsemblFungi; YPR162C_mRNA; YPR162C; YPR162C.
DR   GeneID; 856291; -.
DR   KEGG; sce:YPR162C; -.
DR   AGR; SGD:S000006366; -.
DR   SGD; S000006366; ORC4.
DR   VEuPathDB; FungiDB:YPR162C; -.
DR   eggNOG; KOG2228; Eukaryota.
DR   GeneTree; ENSGT00390000016542; -.
DR   HOGENOM; CLU_007115_4_0_1; -.
DR   InParanoid; P54791; -.
DR   OMA; QRIIYMP; -.
DR   OrthoDB; 230201at2759; -.
DR   BioCyc; YEAST:G3O-34291-MONOMER; -.
DR   Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-SCE-68689; CDC6 association with the ORC:origin complex.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   BioGRID-ORCS; 856291; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P54791; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P54791; Protein.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:SGD.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IDA:SGD.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR016527; ORC4.
DR   InterPro; IPR032705; ORC4_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12087; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR   PANTHER; PTHR12087:SF0; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR   Pfam; PF14629; ORC4_C; 1.
DR   PIRSF; PIRSF007858; ORC4; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA replication; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..529
FT                   /note="Origin recognition complex subunit 4"
FT                   /id="PRO_0000127091"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   HELIX           47..61
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           73..90
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           108..120
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          124..133
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           141..155
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           177..187
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          223..226
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           229..240
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          245..252
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           256..259
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           262..267
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           281..292
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           302..314
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           319..330
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           334..346
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           351..360
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           362..371
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   TURN            372..374
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           376..380
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           385..400
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          401..404
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           408..424
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           453..465
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          468..471
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           481..488
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           493..495
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           499..501
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   STRAND          504..508
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           510..516
FT                   /evidence="ECO:0007829|PDB:7TJF"
FT   HELIX           524..527
FT                   /evidence="ECO:0007829|PDB:7TJF"
SQ   SEQUENCE   529 AA;  60705 MW;  ACF064F2C633F13F CRC64;
     MTISEARLSP QVNLLPIKRH SNEEVEETAA ILKKRTIDNE KCKDSDPGFG SLQRRLLQQL
     YGTLPTDEKI IFTYLQDCQQ EIDRIIKQSI IQKESHSVIL VGPRQSYKTY LLDYELSLLQ
     QSYKEQFITI RLNGFIHSEQ TAINGIATQL EQQLQKIHGS EEKIDDTSLE TISSGSLTEV
     FEKILLLLDS TTKTRNEDSG EVDRESITKI TVVFIFDEID TFAGPVRQTL LYNLFDMVEH
     SRVPVCIFGC TTKLNILEYL EKRVKSRFSQ RVIYMPQIQN LDDMVDAVRN LLTVRSEISP
     WVSQWNETLE KELSDPRSNL NRHIRMNFET FRSLPTLKNS IIPLVATSKN FGSLCTAIKS
     CSFLDIYNKN QLSNNLTGRL QSLSDLELAI LISAARVALR AKDGSFNFNL AYAEYEKMIK
     AINSRIPTVA PTTNVGTGQS TFSIDNTIKL WLKKDVKNVW ENLVQLDFFT EKSAVGLRDN
     ATAAFYASNY QFQGTMIPFD LRSYQMQIIL QELRRIIPKS NMYYSWTQL
//