ORC6_YEAST
ID ORC6_YEAST Reviewed; 435 AA.
AC P38826; D3DL68;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Origin recognition complex subunit 6;
DE AltName: Full=ACS-associated protein 1;
DE AltName: Full=Origin recognition complex 50 kDa subunit;
GN Name=ORC6; Synonyms=AAP1; OrderedLocusNames=YHR118C;
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=8266075; DOI=10.1126/science.8266075;
RA Li J.J., Herskowitz I.;
RT "Isolation of ORC6, a component of the yeast origin recognition complex by
RT a one-hybrid system.";
RL Science 262:1870-1874(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [5]
RP FUNCTION, AND INTERACTION WITH TAH11.
RX PubMed=17825064; DOI=10.1111/j.1567-1364.2007.00299.x;
RA Asano T., Makise M., Takehara M., Mizushima T.;
RT "Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:1256-1262(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH ORC3; ORC5 AND TAH11.
RX PubMed=18006685; DOI=10.1101/gad.1596807;
RA Chen S., de Vries M.A., Bell S.P.;
RT "Orc6 is required for dynamic recruitment of Cdt1 during repeated Mcm2-7
RT loading.";
RL Genes Dev. 21:2897-2907(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146, AND IDENTIFICATION BY
RP MASS 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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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. {ECO:0000269|PubMed:17825064,
CC ECO:0000269|PubMed:18006685}.
CC -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with ORC3,
CC ORC5 and TAH11. {ECO:0000269|PubMed:17825064,
CC ECO:0000269|PubMed:18006685}.
CC -!- INTERACTION:
CC P38826; Q00684: CDC14; NbExp=2; IntAct=EBI-12588, EBI-4192;
CC P38826; P24869: CLB2; NbExp=2; IntAct=EBI-12588, EBI-4515;
CC P38826; P54784: ORC1; NbExp=4; IntAct=EBI-12588, EBI-12568;
CC P38826; P32833: ORC2; NbExp=6; IntAct=EBI-12588, EBI-12572;
CC P38826; P54790: ORC3; NbExp=4; IntAct=EBI-12588, EBI-12576;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 2970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ORC6 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L23323; AAA21822.1; -; Genomic_DNA.
DR EMBL; U00059; AAB68869.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06812.1; -; Genomic_DNA.
DR PIR; A49387; A49387.
DR RefSeq; NP_011986.1; NM_001179248.1.
DR PDB; 5V8F; EM; 3.90 A; F=1-435.
DR PDB; 5ZR1; EM; 3.00 A; F=1-435.
DR PDB; 6RQC; EM; 4.40 A; F=1-435.
DR PDB; 6WGC; EM; 4.30 A; F=1-435.
DR PDB; 6WGG; EM; 8.10 A; F=1-435.
DR PDB; 6WGI; EM; 10.00 A; F=1-435.
DR PDB; 7MCA; EM; 3.60 A; F=1-435.
DR PDBsum; 5V8F; -.
DR PDBsum; 5ZR1; -.
DR PDBsum; 6RQC; -.
DR PDBsum; 6WGC; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7MCA; -.
DR AlphaFoldDB; P38826; -.
DR SMR; P38826; -.
DR BioGRID; 36551; 498.
DR ComplexPortal; CPX-768; Nuclear origin recognition complex.
DR DIP; DIP-2289N; -.
DR ELM; P38826; -.
DR IntAct; P38826; 21.
DR MINT; P38826; -.
DR STRING; 4932.YHR118C; -.
DR iPTMnet; P38826; -.
DR MaxQB; P38826; -.
DR PaxDb; P38826; -.
DR PRIDE; P38826; -.
DR EnsemblFungi; YHR118C_mRNA; YHR118C; YHR118C.
DR GeneID; 856518; -.
DR KEGG; sce:YHR118C; -.
DR SGD; S000001160; ORC6.
DR VEuPathDB; FungiDB:YHR118C; -.
DR eggNOG; ENOG502QS52; Eukaryota.
DR HOGENOM; CLU_660677_0_0_1; -.
DR InParanoid; P38826; -.
DR OMA; ARYHICA; -.
DR BioCyc; YEAST:G3O-31160-MON; -.
DR PRO; PR:P38826; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38826; 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; IC: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 assembly; IDA:SGD.
DR InterPro; IPR008721; ORC6.
DR InterPro; IPR016811; ORC6_fun.
DR Pfam; PF05460; ORC6; 1.
DR PIRSF; PIRSF022941; ORC6_fun; 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..435
FT /note="Origin recognition complex subunit 6"
FT /id="PRO_0000127102"
FT REGION 106..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 394..402
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 415..429
FT /evidence="ECO:0007829|PDB:5ZR1"
SQ SEQUENCE 435 AA; 50296 MW; 22803C70378B7E85 CRC64;
MSMQQVQHCV AEVLRLDPQE KPDWSSGYLK KLTNATSILY NTSLNKVMLK QDEEVARCHI
CAYIASQKMN EKHMPDLCYY IDSIPLEPKK AKHLMNLFRQ SLSNSSPMKQ FAWTPSPKKN
KRSPVKNGGR FTSSDPKELR NQLFGTPTKV RKSQNNDSFV IPELPPMQTN ESPSITRRKL
AFEEDEDEDE EEPGNDGLSL KSHSNKSITG TRNVDSDEYE NHESDPTSEE EPLGVQESRS
GRTKQNKAVG KPQSELKTAK ALRKRGRIPN SLLVKKYCKM TTEEIIRLCN DFELPREVAY
KIVDEYNINA SRLVCPWQLV CGLVLNCTFI VFNERRRKDP RIDHFIVSKM CSLMLTSKVD
DVIECVKLVK ELIIGEKWFR DLQIRYDDFD GIRYDEIIFR KLGSMLQTTN ILVTDDQYNI
WKKRIEMDLA LTEPL
