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RLF2_SCHPO
ID   RLF2_SCHPO              Reviewed;         544 AA.
AC   Q1MTN9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Chromatin assembly factor 1 subunit rlf2;
GN   Name=rlf2; ORFNames=SPBC29A10.03c;
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 [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   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Acts as a component of chromatin assembly factor 1 (CAF-1),
CC       which assembles histone octamers onto replicating DNA in vitro. It
CC       performs the first step of the nucleosome assembly process, bringing
CC       newly synthesized histones H3 and H4 to replicating DNA; histones
CC       H2A/H2B can bind to this chromatin precursor subsequent to DNA
CC       replication to complete the histone octamer. May facilitate the
CC       efficient and timely assembly of histones into telomeric chromatin (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of chromatin assembly factor 1 (CAF-1).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q1MTN9; Q03392: pcn1; NbExp=4; IntAct=EBI-1560762, EBI-768724;
CC       Q1MTN9; O13985: SPAC26H5.03; NbExp=2; IntAct=EBI-1560762, EBI-16123749;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the RLF2 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB44771.2; -; Genomic_DNA.
DR   RefSeq; NP_596048.2; NM_001021958.3.
DR   AlphaFoldDB; Q1MTN9; -.
DR   SMR; Q1MTN9; -.
DR   BioGRID; 277081; 15.
DR   DIP; DIP-38719N; -.
DR   IntAct; Q1MTN9; 4.
DR   STRING; 4896.SPBC29A10.03c.1; -.
DR   MaxQB; Q1MTN9; -.
DR   PaxDb; Q1MTN9; -.
DR   PRIDE; Q1MTN9; -.
DR   EnsemblFungi; SPBC29A10.03c.1; SPBC29A10.03c.1:pep; SPBC29A10.03c.
DR   GeneID; 2540554; -.
DR   KEGG; spo:SPBC29A10.03c; -.
DR   PomBase; SPBC29A10.03c; -.
DR   VEuPathDB; FungiDB:SPBC29A10.03c; -.
DR   eggNOG; KOG4363; Eukaryota.
DR   HOGENOM; CLU_013392_1_0_1; -.
DR   InParanoid; Q1MTN9; -.
DR   OMA; YQGTFTK; -.
DR   PhylomeDB; Q1MTN9; -.
DR   PRO; PR:Q1MTN9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0033186; C:CAF-1 complex; IDA:PomBase.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0043596; C:nuclear replication fork; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IMP:PomBase.
DR   GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IDA:PomBase.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   InterPro; IPR022043; CAF1A.
DR   Pfam; PF12253; CAF1A; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Reference proteome.
FT   CHAIN           1..544
FT                   /note="Chromatin assembly factor 1 subunit rlf2"
FT                   /id="PRO_0000372425"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..176
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..389
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  62278 MW;  B7413523836A9C4A CRC64;
     MNSESVDSDV AASTSNKGNE LCSSSTDITS LSVSSPNESV IHSSHSASEA DEYVCKLSYE
     GNRKKRIYNG SAEAGKEKKL QKQRAQEERI RQKEAERLKR EKERQQREQE KKLREQEKIA
     AKKMKELEKL EKERIRLQEQ QRRKEERDQK LREKEEAQRL RQEQILNKER QQLKLNNFFT
     KGVEKRIAPN ENFVADKTDE LNEFEKEFRP FFIKHQMSLS KYPSPNESDS FLDEVLSTSK
     SYPLKLNDIF TPSDAVSSAN SLGVSNRNSE NEVRQLMSAY QDPSVSKPQE ILSCLSQIPI
     KFIFFYQDVR PPYFGSYTKT HSHGSNVLLN PWLEDEDIDY TYDSEAEWVA DEEDDGEDLE
     SEDEEVDNSD DIVEDGDNAF VDDEDDDKDS VNASNTHRSS GPLEVIVEGP VWDSKFLPDF
     NCLSLIEPIS SFSASTYLQI DPKEDLWASQ DTAPASSGMT IGPTSSLSDD LQVRFPSEDI
     PKFIEYVRNS HDNKVFLIEN LRHMFPYVTK NIISETLGKV AVRKGKSVSD GWIIKENFAS
     LLSS
 
 
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