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ORC5_DROME
ID   ORC5_DROME              Reviewed;         460 AA.
AC   Q24169; Q9V398;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Origin recognition complex subunit 5;
GN   Name=Orc5; ORFNames=CG7833;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7502079; DOI=10.1126/science.270.5242.1674;
RA   Gossen M., Pak D.T.S., Hansen S.K., Acharya J.K., Botchan M.R.;
RT   "A Drosophila homolog of the yeast origin recognition complex.";
RL   Science 270:1674-1677(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA   Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA   Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA   Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA   Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA   Celniker S.E., Rubin G.M.;
RT   "An exploration of the sequence of a 2.9-Mb region of the genome of
RT   Drosophila melanogaster: the Adh region.";
RL   Genetics 153:179-219(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC       origins of replication. DNA-binding is ATP-dependent, however specific
CC       DNA sequences that define origins of replication have not been
CC       identified so far. ORC is required to assemble the pre-replication
CC       complex necessary to initiate DNA replication (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: ORC is composed of six subunits.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ORC5 family. {ECO:0000305}.
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DR   EMBL; U43505; AAC46956.1; -; mRNA.
DR   EMBL; AE014134; AAF53340.1; -; Genomic_DNA.
DR   EMBL; AY089590; AAL90328.1; -; mRNA.
DR   RefSeq; NP_477132.1; NM_057784.8.
DR   PDB; 4XGC; X-ray; 3.50 A; E=1-460.
DR   PDB; 7JGR; EM; 3.90 A; E=1-460.
DR   PDB; 7JGS; EM; 3.20 A; E=1-460.
DR   PDB; 7JK2; EM; 3.20 A; E=1-460.
DR   PDB; 7JK3; EM; 3.40 A; E=1-460.
DR   PDB; 7JK4; EM; 3.40 A; E=1-460.
DR   PDB; 7JK5; EM; 3.90 A; E=1-460.
DR   PDB; 7JK6; EM; 4.00 A; E=1-460.
DR   PDBsum; 4XGC; -.
DR   PDBsum; 7JGR; -.
DR   PDBsum; 7JGS; -.
DR   PDBsum; 7JK2; -.
DR   PDBsum; 7JK3; -.
DR   PDBsum; 7JK4; -.
DR   PDBsum; 7JK5; -.
DR   PDBsum; 7JK6; -.
DR   AlphaFoldDB; Q24169; -.
DR   SMR; Q24169; -.
DR   BioGRID; 60827; 13.
DR   DIP; DIP-49320N; -.
DR   IntAct; Q24169; 4.
DR   STRING; 7227.FBpp0080120; -.
DR   PaxDb; Q24169; -.
DR   DNASU; 34794; -.
DR   EnsemblMetazoa; FBtr0080543; FBpp0080120; FBgn0015271.
DR   GeneID; 34794; -.
DR   KEGG; dme:Dmel_CG7833; -.
DR   CTD; 5001; -.
DR   FlyBase; FBgn0015271; Orc5.
DR   VEuPathDB; VectorBase:FBgn0015271; -.
DR   eggNOG; KOG2543; Eukaryota.
DR   GeneTree; ENSGT00390000009380; -.
DR   HOGENOM; CLU_028223_0_1_1; -.
DR   InParanoid; Q24169; -.
DR   OMA; QLRRWHG; -.
DR   OrthoDB; 571556at2759; -.
DR   PhylomeDB; Q24169; -.
DR   Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-DME-68689; CDC6 association with the ORC:origin complex.
DR   Reactome; R-DME-68949; Orc1 removal from chromatin.
DR   Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR   SignaLink; Q24169; -.
DR   BioGRID-ORCS; 34794; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 34794; -.
DR   PRO; PR:Q24169; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0015271; Expressed in secondary oocyte and 34 other tissues.
DR   Genevisible; Q24169; DM.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IMP:FlyBase.
DR   GO; GO:0006270; P:DNA replication initiation; IDA:FlyBase.
DR   GO; GO:0006261; P:DNA-templated DNA replication; ISS:FlyBase.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR020796; ORC5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12705; PTHR12705; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF14630; ORC5_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..460
FT                   /note="Origin recognition complex subunit 5"
FT                   /id="PRO_0000127094"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   HELIX           2..11
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          35..41
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:7JK2"
FT   HELIX           48..61
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          62..70
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           77..88
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:7JK3"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           128..133
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          151..161
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           185..193
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           196..205
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           212..219
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           223..237
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            238..240
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           244..258
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           276..287
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            288..291
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           323..337
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           343..347
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            373..375
FT                   /evidence="ECO:0007829|PDB:4XGC"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:4XGC"
FT   HELIX           382..393
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           401..412
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          415..420
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          422..424
FT                   /evidence="ECO:0007829|PDB:7JK2"
FT   TURN            425..428
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   STRAND          431..434
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   HELIX           438..448
FT                   /evidence="ECO:0007829|PDB:7JGS"
FT   TURN            453..455
FT                   /evidence="ECO:0007829|PDB:7JGS"
SQ   SEQUENCE   460 AA;  52115 MW;  FDCE3969E1CBF7D2 CRC64;
     MEAICSSLEP LFPCREAAIE TLGELIGDSS ETYPSAIYLF GHSGTGKTAL TRAFLKECGK
     RQNVRTAHLN AIECYTTKIM LEILLDSLAP DQGDALKVDN MLDFVEQLRR QAATRVEDQG
     FLIAVDNAER LRDMDANVLP VLLRLQELTN LNLCVILLSQ LPFEKFYNKT GLSEIVCLHL
     AQYNKAETQR ILGSDFQQVR NQLLEQFAQD KKRLEICQEA VTEDFYNNYL NLFLSVFYKA
     CRDVPELQLT ARKCLSTYLE PVLDGTVDAT DISRLWRHIA GPLRSALTQI YMRIEKPAEE
     VEDFTAIEDQ SVRKLAQSLE LPYYAKFLLI AAFLASHNAA KQDKRLFVKH HGKQRKRMQT
     VNARAKTTEK MSTTLGPKSF SIDRLLAIFY AILEEKVGLT CNLLSQISTL VHLNLLSFVS
     GEQNIMEGSA RLQCTIGLEF VLQIGKVVGF NVRQYLCDFM
 
 
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