BRC1_SCHPO
ID BRC1_SCHPO Reviewed; 878 AA.
AC Q10337;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=BRCT-containing protein 1;
GN Name=brc1; ORFNames=SPBC582.05c;
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 FUNCTION.
RX PubMed=10473635; DOI=10.1091/mbc.10.9.2905;
RA Verkade H.M., Bugg S.J., Lindsay H.D., Carr A.M., O'Connell M.J.;
RT "Rad18 is required for DNA repair and checkpoint responses in fission
RT yeast.";
RL Mol. Biol. Cell 10:2905-2918(1999).
CC -!- FUNCTION: Required for mitotic fidelity, specifically in the G2 phase
CC of the cell cycle. Plays a role in chromatin organization.
CC {ECO:0000269|PubMed:10473635}.
CC -!- INTERACTION:
CC Q10337; P04909: hta1; NbExp=4; IntAct=EBI-7764855, EBI-7764873;
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DR EMBL; CU329671; CAB46668.1; -; Genomic_DNA.
DR PIR; T37978; T37978.
DR RefSeq; NP_595173.1; NM_001021081.1.
DR PDB; 3L40; X-ray; 1.55 A; A/B=659-877.
DR PDB; 3L41; X-ray; 1.45 A; A=659-878.
DR PDBsum; 3L40; -.
DR PDBsum; 3L41; -.
DR AlphaFoldDB; Q10337; -.
DR SMR; Q10337; -.
DR BioGRID; 277586; 67.
DR IntAct; Q10337; 1.
DR MINT; Q10337; -.
DR STRING; 4896.SPBC582.05c.1; -.
DR iPTMnet; Q10337; -.
DR MaxQB; Q10337; -.
DR PaxDb; Q10337; -.
DR PRIDE; Q10337; -.
DR EnsemblFungi; SPBC582.05c.1; SPBC582.05c.1:pep; SPBC582.05c.
DR GeneID; 2541071; -.
DR KEGG; spo:SPBC582.05c; -.
DR PomBase; SPBC582.05c; brc1.
DR VEuPathDB; FungiDB:SPBC582.05c; -.
DR eggNOG; KOG2043; Eukaryota.
DR HOGENOM; CLU_328771_0_0_1; -.
DR InParanoid; Q10337; -.
DR OMA; IKIVLPH; -.
DR PhylomeDB; Q10337; -.
DR EvolutionaryTrace; Q10337; -.
DR PRO; PR:Q10337; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0006301; P:postreplication repair; IMP:PomBase.
DR Gene3D; 3.40.50.10190; -; 5.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 6.
DR SUPFAM; SSF52113; SSF52113; 4.
DR PROSITE; PS50172; BRCT; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat.
FT CHAIN 1..878
FT /note="BRCT-containing protein 1"
FT /id="PRO_0000064983"
FT DOMAIN 14..104
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 105..196
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 311..399
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 654..744
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 767..872
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 482..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 681..686
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:3L41"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 709..714
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 724..733
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 747..753
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 757..767
FT /evidence="ECO:0007829|PDB:3L41"
FT TURN 771..774
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 775..780
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 811..819
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 822..826
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 831..834
FT /evidence="ECO:0007829|PDB:3L41"
FT TURN 835..837
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 838..841
FT /evidence="ECO:0007829|PDB:3L41"
FT STRAND 847..851
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 852..861
FT /evidence="ECO:0007829|PDB:3L41"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:3L41"
SQ SEQUENCE 878 AA; 98436 MW; AFCAFBEF800CBFC6 CRC64;
MEKIKLLNVK TPNHYTIIFK VVAYYSALQP NQNELRKKEL FIKNDGKALS FPYDWKLATH
VICDDFSSPN VQEGSKRSLR LAKTNWIRDC VDKNTLLNYS FYSCNPYLLF KGICASSCQI
DSYQSSLIDD ALETFGGRFS KGLMKSMTHL FTYSGMGAKC KKVLDKPSLS IKLIHPQWLL
DCLQFGQLID QDPYLFPNPS YKKNDSSISK AEPTSLFRNV LHGKRIYFSN DLNLPTNFRH
SLQKFSVGIG AKIAESINDC DIFIGLKRDT IEFNLASNKN TTIGTISWLL NLFVLGSWKS
PLLNALHYPF PSVGFLKDQM VAVTNYTDAA RIYLEKLLLA CGATYTKDLK PTNTLLIAAS
SYGQKYGAAK VWNIPTVHHS WLYSSFKNLS SQAFTDFPVP LDDSYMDFIF PCPLNVEKGS
FEDTLKSSLT KGNSEVLLDD LSDPSVSSIK GNKTNEELEK EFKSTSDNFG KHIILTSSFS
NQSADKGSSL AAEDDRNDEG STITGVNREL QDEGRLEIDA KSSKTNTPPS PLLVGTPSKE
SLKEASSDDE LPVLATKLVD NVIKEKSPLS LTPKVVVPSH KETYTDEKKL IDELDRVNPL
NSSQLLRSKR KSAATALSML QNVIMPDVLA FEREKKRRQT HRSVSSGEVS RESSESRNTN
AKASKRVYIT FTGYDKKPSI DNLKKLDMSI TSNPSKCTHL IAPRILRTSK FLCSIPYGPC
VVTMDWINSC LKTHEIVDEE PYLLNDPEKE LELGCTLESA LKRARAQGPS LLEDYVVYLT
SKTVAPENVP AVISIVKSNG GVCSTLNVYN KRLARHLEDG NVVLITCNED SHIWTNFLDN
ASQNKTIFLQ NYDWLIKTVL RQEIDVNDRI ADEFARAV
