ORC5_YEAST
ID ORC5_YEAST Reviewed; 479 AA.
AC P50874; D6W0T2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Origin recognition complex subunit 5;
DE AltName: Full=Origin recognition complex 53 kDa subunit;
GN Name=ORC5; OrderedLocusNames=YNL261W; ORFNames=N0834;
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 PROTEIN SEQUENCE OF 87-102; 111-125;
RP 276-286 AND 416-431.
RX PubMed=7579692; DOI=10.1091/mbc.6.6.741;
RA Loo S., Fox C.A., Rine J., Kobayashi R., Stillman B., Bell S.P.;
RT "The origin recognition complex in silencing, cell cycle progression, and
RT DNA replication.";
RL Mol. Biol. Cell 6:741-756(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [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 FUNCTION, AND INTERACTION WITH ORC6.
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 IN A COMPLEX WITH RTT101 AND MMS1.
RX PubMed=20139071; DOI=10.1074/jbc.m109.082107;
RA Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C.,
RA Kamura T.;
RT "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage
RT response and transcriptional silencing.";
RL J. Biol. Chem. 285:9858-9867(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. This subunit is a candidate
CC for the mediation of ATP-dependent binding of ORC to origins. May also
CC be a substrate targeting component of a cullin-RING-based E3 ubiquitin-
CC protein ligase complex RTT101(MMS1-ORC5).
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 ORC6.
CC Component of a cullin-RING ligase (CRL)-like complex composed of at
CC least the cullin RTT101, a linker protein MMS1, and the potential
CC substrate receptor ORC5. Interacts with RTT101 and MMS1.
CC {ECO:0000269|PubMed:18006685, ECO:0000269|PubMed:20139071}.
CC -!- INTERACTION:
CC P50874; Q06211: MMS1; NbExp=4; IntAct=EBI-12584, EBI-38894;
CC P50874; P32833: ORC2; NbExp=4; IntAct=EBI-12584, EBI-12572;
CC P50874; P54791: ORC4; NbExp=9; IntAct=EBI-12584, EBI-12580;
CC P50874; P47050: RTT101; NbExp=3; IntAct=EBI-12584, EBI-25861;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ORC5 family. {ECO:0000305}.
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DR EMBL; U24187; AAC49122.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65483.1; -; Genomic_DNA.
DR EMBL; Z71537; CAA96168.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10298.1; -; Genomic_DNA.
DR PIR; S61768; S61768.
DR RefSeq; NP_014138.1; NM_001183099.1.
DR PDB; 5V8F; EM; 3.90 A; E=1-479.
DR PDB; 5ZR1; EM; 3.00 A; E=1-479.
DR PDB; 6RQC; EM; 4.40 A; E=1-479.
DR PDB; 6WGC; EM; 4.30 A; E=1-479.
DR PDB; 6WGG; EM; 8.10 A; E=1-479.
DR PDB; 6WGI; EM; 10.00 A; E=1-479.
DR PDB; 7MCA; EM; 3.60 A; E=1-479.
DR PDBsum; 5V8F; -.
DR PDBsum; 5ZR1; -.
DR PDBsum; 6RQC; -.
DR PDBsum; 6WGC; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7MCA; -.
DR AlphaFoldDB; P50874; -.
DR SMR; P50874; -.
DR BioGRID; 35578; 128.
DR ComplexPortal; CPX-1167; CUL8-MMS1-ORC5 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-768; Nuclear origin recognition complex.
DR DIP; DIP-2288N; -.
DR IntAct; P50874; 18.
DR MINT; P50874; -.
DR STRING; 4932.YNL261W; -.
DR MaxQB; P50874; -.
DR PaxDb; P50874; -.
DR PRIDE; P50874; -.
DR TopDownProteomics; P50874; -.
DR EnsemblFungi; YNL261W_mRNA; YNL261W; YNL261W.
DR GeneID; 855460; -.
DR KEGG; sce:YNL261W; -.
DR SGD; S000005205; ORC5.
DR VEuPathDB; FungiDB:YNL261W; -.
DR eggNOG; KOG2543; Eukaryota.
DR GeneTree; ENSGT00390000009380; -.
DR HOGENOM; CLU_028223_2_1_1; -.
DR InParanoid; P50874; -.
DR OMA; PIELVSW; -.
DR BioCyc; YEAST:G3O-33257-MON; -.
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-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR PRO; PR:P50874; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P50874; protein.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IC:ComplexPortal.
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:0005524; F:ATP binding; IMP:SGD.
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:0006275; P:regulation of DNA replication; IC:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020796; ORC5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12705; PTHR12705; 1.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF14630; ORC5_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA replication;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..479
FT /note="Origin recognition complex subunit 5"
FT /id="PRO_0000127096"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 229..251
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:5ZR1"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:5ZR1"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:5ZR1"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5ZR1"
SQ SEQUENCE 479 AA; 55289 MW; 1FE5DE28AFF6B41C CRC64;
MNVTTPEVAF REYQTNCLAS YISADPDITP SNLILQGYSG TGKTYTLKKY FNANPNLHAV
WLEPVELVSW KPLLQAIART VQYKLKTLYP NIPTTDYDPL QVEEPFLLVK TLHNIFVQYE
SLQEKTCLFL ILDGFDSLQD LDAALFNKYI KLNELLPKDS KINIKFIYTM LETSFLQRYS
THCIPTVMFP RYNVDEVSTI LVMSRCGELM EDSCLRKRII EEQITDCTDD QFQNVAANFI
HLIVQAFHSY TGNDIFALND LIDFKWPKYV SRITKENIFE PLALYKSAIK LFLSTDDNLS
ENGQGESAIT TNRDDLENSQ TYDLSIISKY LLIASYICSY LEPRYDASIF SRKTRIIQGR
AAYGRRKKKE VNPRYLQPSL FAIERLLAIF QAIFPIQGKA ESGSLSALRE ESLMKANIEV
FQNLSELHTL KLIATTMNKN IDYLSPKVRW KVNVPWEIIK EISESVHFNI SDYFSDIHE
