RHP9_SCHPO
ID RHP9_SCHPO Reviewed; 778 AA.
AC P87074; Q09754;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA repair protein crb2 {ECO:0000305|PubMed:9407031};
DE AltName: Full=Checkpoint mediator protein crb2 {ECO:0000303|PubMed:24074952};
DE AltName: Full=Cut5-repeat binding protein 2 {ECO:0000303|PubMed:9407031};
DE AltName: Full=RAD9 protein homolog {ECO:0000303|PubMed:9153313};
GN Name=crb2 {ECO:0000303|PubMed:9407031};
GN Synonyms=rhp9 {ECO:0000303|PubMed:9153313};
GN ORFNames=SPBC342.05 {ECO:0000312|PomBase:SPBC342.05};
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9153313; DOI=10.1093/nar/25.11.2138;
RA Willson J., Wilson S., Warr N., Watts F.Z.;
RT "Isolation and characterization of the Schizosaccharomyces pombe rhp9 gene:
RT a gene required for the DNA damage checkpoint but not the replication
RT checkpoint.";
RL Nucleic Acids Res. 25:2138-2145(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND INTERACTION WITH RAD4 AND CHK1.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9407031; DOI=10.1101/gad.11.24.3387;
RA Saka Y., Esashi F., Matsusaka T., Mochida S., Yanagida M.;
RT "Damage and replication checkpoint control in fission yeast is ensured by
RT interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.";
RL Genes Dev. 11:3387-3400(1997).
RN [3]
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 [4]
RP PHOSPHORYLATION AT THR-215 BY CDC2.
RX PubMed=10488332; DOI=10.1016/s1097-2765(00)80364-0;
RA Esashi F., Yanagida M.;
RT "Cdc2 phosphorylation of Crb2 is required for reestablishing cell cycle
RT progression after the damage checkpoint.";
RL Mol. Cell 4:167-174(1999).
RN [5]
RP INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15550243; DOI=10.1016/j.cell.2004.11.009;
RA Sanders S.L., Portoso M., Mata J., Baehler J., Allshire R.C.,
RA Kouzarides T.;
RT "Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites
RT of DNA damage.";
RL Cell 119:603-614(2004).
RN [7]
RP INTERACTION WITH CHK1; RAD3 AND RAD4.
RX PubMed=14739927; DOI=10.1038/sj.emboj.7600018;
RA Mochida S., Esashi F., Aono N., Tamai K., O'Connell M.J., Yanagida M.;
RT "Regulation of checkpoint kinases through dynamic interaction with Crb2.";
RL EMBO J. 23:418-428(2004).
RN [8]
RP PHOSPHORYLATION AT THR-215, AND MUTAGENESIS OF THR-215.
RX PubMed=16314498; DOI=10.1128/mcb.25.24.10721-10730.2005;
RA Nakamura T.M., Moser B.A., Du L.-L., Russell P.;
RT "Cooperative control of Crb2 by ATM family and Cdc2 kinases is essential
RT for the DNA damage checkpoint in fission yeast.";
RL Mol. Cell. Biol. 25:10721-10730(2005).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF THR-235.
RX PubMed=16778077; DOI=10.1101/gad.1422606;
RA Du L.L., Nakamura T.M., Russell P.;
RT "Histone modification-dependent and -independent pathways for recruitment
RT of checkpoint protein Crb2 to double-strand breaks.";
RL Genes Dev. 20:1583-1596(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H4.
RX PubMed=18826944; DOI=10.1074/jbc.m806857200;
RA Greeson N.T., Sengupta R., Arida A.R., Jenuwein T., Sanders S.L.;
RT "Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA
RT damage.";
RL J. Biol. Chem. 283:33168-33174(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H2A.
RX PubMed=20679485; DOI=10.1128/mcb.00413-10;
RA Sofueva S., Du L.L., Limbo O., Williams J.S., Russell P.;
RT "BRCT domain interactions with phospho-histone H2A target Crb2 to chromatin
RT at double-strand breaks and maintain the DNA damage checkpoint.";
RL Mol. Cell. Biol. 30:4732-4743(2010).
RN [12]
RP FUNCTION, INTERACTION WITH CHK1, AND PHOSPHORYLATION AT THR-73 AND SER-80.
RX PubMed=22792081; DOI=10.1371/journal.pgen.1002817;
RA Qu M., Yang B., Tao L., Yates J.R., Russell P., Dong M.Q., Du L.L.;
RT "Phosphorylation-dependent interactions between Crb2 and Chk1 are essential
RT for DNA damage checkpoint.";
RL PLoS Genet. 8:E1002817-E1002817(2012).
RN [13]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PHE-400.
RX PubMed=24806815; DOI=10.1371/journal.pone.0097028;
RA Wei Y., Wang H.T., Zhai Y., Russell P., Du L.L.;
RT "Mdb1, a fission yeast homolog of human MDC1, modulates DNA damage response
RT and mitotic spindle function.";
RL PLoS ONE 9:E97028-E97028(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 358-507, AND INTERACTION WITH
RP HISTONE H4.
RX PubMed=17190600; DOI=10.1016/j.cell.2006.10.043;
RA Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J., Mer G.;
RT "Structural basis for the methylation state-specific recognition of histone
RT H4-K20 by 53BP1 and Crb2 in DNA repair.";
RL Cell 127:1361-1373(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 537-778 IN COMPLEX WITH HISTONE
RP H2A, SUBUNIT, AND MUTAGENESIS OF ARG-616; LYS-617; LYS-619; CYS-663 AND
RP SER-666.
RX PubMed=18676809; DOI=10.1101/gad.472808;
RA Kilkenny M.L., Dore A.S., Roe S.M., Nestoras K., Ho J.C., Watts F.Z.,
RA Pearl L.H.;
RT "Structural and functional analysis of the Crb2-BRCT2 domain reveals
RT distinct roles in checkpoint signaling and DNA damage repair.";
RL Genes Dev. 22:2034-2047(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 180-193 AND OF 229-241,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-187; THR-215 AND THR-235,
RP INTERACTION WITH RAD4, AND MUTAGENESIS OF VAL-184; THR-187; THR-215 AND
RP THR-235.
RX PubMed=24074952; DOI=10.1016/j.molcel.2013.08.030;
RA Qu M., Rappas M., Wardlaw C.P., Garcia V., Ren J.Y., Day M., Carr A.M.,
RA Oliver A.W., Du L.L., Pearl L.H.;
RT "Phosphorylation-dependent assembly and coordination of the DNA damage
RT checkpoint apparatus by Rad4(TopBP1).";
RL Mol. Cell 51:723-736(2013).
CC -!- FUNCTION: Essential for cell cycle arrest at the G1 and G2 stages
CC following DNA damage by X-, and UV-irradiation, or inactivation of DNA
CC ligase. Plays a role in the response to DNA damage (PubMed:9153313,
CC PubMed:9407031). Interaction with rad4 via its phosphorylation sites in
CC the N-terminus couples the DNA checkpoint apparatus to chromatin via
CC interaction of its C-terminal BRCT domains with epigenetic
CC modifications on histones H4 and H2A, respectively, in the G1/S phase
CC of the cell cycle, and facilitates recruitment of the checkpoint kinase
CC chk1 (PubMed:15550243, PubMed:16778077, PubMed:18826944,
CC PubMed:20679485, PubMed:22792081). {ECO:0000269|PubMed:15550243,
CC ECO:0000269|PubMed:16778077, ECO:0000269|PubMed:18826944,
CC ECO:0000269|PubMed:20679485, ECO:0000269|PubMed:22792081,
CC ECO:0000269|PubMed:9153313, ECO:0000269|PubMed:9407031}.
CC -!- SUBUNIT: Homodimer. Dimerization is mediated via the BRCT domain
CC (PubMed:16778077, PubMed:18676809). Interacts (via BRCT domain) with
CC rad3 (PubMed:14739927). Interacts with rad4 (via BRCT1,2 domains)
CC (PubMed:9407031, PubMed:14739927); a single rad4 molecule interacts
CC simultaneously with both Thr-187 phosphorylation sites in a crb2 dimer
CC (PubMed:24074952). Interacts (via Tudor domain) with histone H4K20me2
CC (PubMed:18826944, PubMed:17190600). Interacts (via BRCT dmain) with
CC histone H2AS128ph (gamma-H2A) (PubMed:20679485, PubMed:18676809).
CC Interacts with chk1 (PubMed:9407031, PubMed:14739927, PubMed:22792081).
CC Interacts with sad1 (PubMed:14655046). {ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:14739927, ECO:0000269|PubMed:16778077,
CC ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:18676809,
CC ECO:0000269|PubMed:18826944, ECO:0000269|PubMed:20679485,
CC ECO:0000269|PubMed:24074952, ECO:0000269|PubMed:9407031,
CC ECO:0000305|PubMed:22792081}.
CC -!- INTERACTION:
CC P87074; P34208: chk1; NbExp=4; IntAct=EBI-768448, EBI-768535;
CC P87074; P87074: crb2; NbExp=3; IntAct=EBI-768448, EBI-768448;
CC P87074; Q02099: rad3; NbExp=3; IntAct=EBI-768448, EBI-768555;
CC P87074; P32372: rad4; NbExp=2; IntAct=EBI-768448, EBI-768521;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:15550243, ECO:0000269|PubMed:9407031}.
CC Note=Recruited to sites of DNA damage, such as double stand breaks.
CC {ECO:0000269|PubMed:18826944, ECO:0000269|PubMed:20679485,
CC ECO:0000269|PubMed:24074952}.
CC -!- DOMAIN: The Tudor-like region mediates binding to H4K20me2.
CC {ECO:0000305|PubMed:17190600}.
CC -!- PTM: Phosphorylation of Thr-73 and Ser-80 by rad3/ATM promotes
CC interaction with chk1 (PubMed:22792081). Phosphorylation at Thr-187 is
CC dependent on phosphorylation at Thr-215 and Thr-235. Phosphorylation at
CC Thr-215 and Thr-235 may prime the non-canonical Thr-187 site for
CC cdc2/CDK phosphorylation (PubMed:24074952).
CC {ECO:0000305|PubMed:22792081, ECO:0000305|PubMed:24074952}.
CC -!- DISRUPTION PHENOTYPE: Not resistant to the microtubule depolymerizing
CC drug thiabendazole (TBZ). DNA damage sensitive in response to ionizing
CC radiation (IR), ultraviolet (UV), hydroxyurea (HU) and camptothecin
CC (CPT). {ECO:0000269|PubMed:24806815}.
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DR EMBL; Y09431; CAA70582.1; -; Genomic_DNA.
DR EMBL; D86478; BAA13093.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB46775.1; -; Genomic_DNA.
DR PIR; T43223; T43223.
DR PIR; T45221; T45221.
DR RefSeq; NP_596748.1; NM_001023768.2.
DR PDB; 2FHD; X-ray; 2.40 A; A/B/C=358-507.
DR PDB; 2VXB; X-ray; 2.30 A; A/B=538-778.
DR PDB; 2VXC; X-ray; 3.10 A; A/B=537-778.
DR PDB; 4BU0; X-ray; 1.50 A; B/C=180-193.
DR PDB; 4BU1; X-ray; 2.10 A; C/D=229-241.
DR PDBsum; 2FHD; -.
DR PDBsum; 2VXB; -.
DR PDBsum; 2VXC; -.
DR PDBsum; 4BU0; -.
DR PDBsum; 4BU1; -.
DR AlphaFoldDB; P87074; -.
DR SMR; P87074; -.
DR BioGRID; 277508; 120.
DR IntAct; P87074; 7.
DR STRING; 4896.SPBC342.05.1; -.
DR iPTMnet; P87074; -.
DR PaxDb; P87074; -.
DR PRIDE; P87074; -.
DR EnsemblFungi; SPBC342.05.1; SPBC342.05.1:pep; SPBC342.05.
DR GeneID; 2540992; -.
DR KEGG; spo:SPBC342.05; -.
DR PomBase; SPBC342.05; crb2.
DR VEuPathDB; FungiDB:SPBC342.05; -.
DR eggNOG; KOG3548; Eukaryota.
DR HOGENOM; CLU_351305_0_0_1; -.
DR InParanoid; P87074; -.
DR OMA; FEWIIEC; -.
DR PhylomeDB; P87074; -.
DR Reactome; R-SPO-3232118; SUMOylation of transcription factors.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR EvolutionaryTrace; P87074; -.
DR PRO; PR:P87074; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0140463; F:chromatin-protein adaptor; IPI:PomBase.
DR GO; GO:0042393; F:histone binding; IPI:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:PomBase.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IGI:PomBase.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041297; Crb2_Tudor.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF18115; Tudor_3; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA damage; DNA replication inhibitor; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..778
FT /note="DNA repair protein crb2"
FT /id="PRO_0000097328"
FT DOMAIN 535..653
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..245
FT /note="Interaction with rad4"
FT /evidence="ECO:0000269|PubMed:16778077"
FT REGION 358..493
FT /note="Tudor-like"
FT /evidence="ECO:0000305|PubMed:17190600"
FT REGION 370..404
FT /note="Interaction with dimethylated histone H4"
FT /evidence="ECO:0000305|PubMed:17190600"
FT MOD_RES 73
FT /note="Phosphothreonine; by ATM"
FT /evidence="ECO:0000305|PubMed:22792081"
FT MOD_RES 80
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:22792081"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24074952"
FT MOD_RES 215
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:10488332,
FT ECO:0000269|PubMed:16314498, ECO:0000269|PubMed:24074952"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24074952"
FT MUTAGEN 73
FT /note="T->A: In crb2-2AQ; abrogates DSB-focus formation by
FT chk1, but not crb2; when associated with A-80."
FT /evidence="ECO:0000269|PubMed:22792081"
FT MUTAGEN 80
FT /note="S->A: In crb2-2AQ; abrogates DSB-focus formation by
FT chk1, but not crb2; when associated with A-73."
FT /evidence="ECO:0000269|PubMed:22792081"
FT MUTAGEN 184
FT /note="V->A: Abolishes formation of radiation-induced crb2
FT foci at DSB sites. Severely impairs checkpoint response
FT after DNA damage."
FT /evidence="ECO:0000269|PubMed:24074952"
FT MUTAGEN 187
FT /note="T->A: Abolishes formation of radiation-induced crb2
FT foci at DSB sites. Severely impairs checkpoint response
FT after DNA damage."
FT /evidence="ECO:0000269|PubMed:24074952"
FT MUTAGEN 188
FT /note="V->P: Transforms T-187 into a consensus CDK
FT phosphorylation site and abolishes the dependence of T-187
FT phosphorylation on prior phosphorylation at T-215 and T-
FT 235."
FT /evidence="ECO:0000269|PubMed:24074952"
FT MUTAGEN 215
FT /note="T->A: Reduces hyper-phosphorylation in response to
FT DNA damage. Abolishes formation of radiation-induced crb2
FT foci at DSB sites. Impairs checkpoint response after DNA
FT damage."
FT /evidence="ECO:0000269|PubMed:16314498,
FT ECO:0000269|PubMed:24074952"
FT MUTAGEN 235
FT /note="T->A: Abolishes formation of radiation-induced crb2
FT foci at DSB sites. Impairs checkpoint response after DNA
FT damage."
FT /evidence="ECO:0000269|PubMed:16778077,
FT ECO:0000269|PubMed:24074952"
FT MUTAGEN 400
FT /note="F->A: Sensitive to DNA damage agent camptothecin
FT (CPT)."
FT /evidence="ECO:0000269|PubMed:24806815"
FT MUTAGEN 616
FT /note="R->E: Disrupts gamma-H2A binding, but has no effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:18676809"
FT MUTAGEN 617
FT /note="K->E: Disrupts gamma-H2A binding, but has no effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:18676809"
FT MUTAGEN 619
FT /note="K->E: Disrupts gamma-H2A binding, but has no effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:18676809"
FT MUTAGEN 663
FT /note="C->R: Disrupts dimer formation, but not gamma-H2A
FT binding."
FT /evidence="ECO:0000269|PubMed:18676809"
FT MUTAGEN 666
FT /note="S->R: Disrupts dimer formation, but not gamma-H2A
FT binding."
FT /evidence="ECO:0000269|PubMed:18676809"
FT CONFLICT 76
FT /note="F -> C (in Ref. 2; BAA13093)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="F -> C (in Ref. 2; BAA13093)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..163
FT /note="LK -> YR (in Ref. 2; BAA13093)"
FT /evidence="ECO:0000305"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4BU1"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:2FHD"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:2FHD"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:2FHD"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:2FHD"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:2FHD"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 558..567
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:2VXB"
FT TURN 584..587
FT /evidence="ECO:0007829|PDB:2VXC"
FT HELIX 599..603
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 618..626
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 634..642
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 652..658
FT /evidence="ECO:0007829|PDB:2VXB"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 678..684
FT /evidence="ECO:0007829|PDB:2VXB"
FT TURN 688..691
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 714..726
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:2VXB"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:2VXB"
FT HELIX 763..772
FT /evidence="ECO:0007829|PDB:2VXB"
SQ SEQUENCE 778 AA; 87462 MW; 5E35178828E6E42A CRC64;
MEVNDTSLHK GFGLDINSQR VFGAQAAISR NNYSKVNASI NPSPPRSNDN SNKEFSYSKD
VNNNGAVEEL SLTQLFEVPS QAAFAKQSSQ DISDDELIQH DSRKVISSPY SPKQTHTVLK
RLYDRQSVIS DHEKLLTPQN VSNSSQILSP FTSLLPSTLS TLKDTPLSVS QNEKNLETVG
EVLVPETVAQ HRTKFYDYTL DEMENETESG QVETTPTRLA TSLGSPVLYG RVESTPPAFL
PETSEKQYKR KFSFTEPSSE KVDNTETKFS KKTKNINDEN FPNPFNVISS YETSASPSTV
IDQSSQVSSI FVNKRLRKSV NNQAISRSDS LSLDTPKIDS LFTRASIKPL KPSQSPNSRR
SFKNRVLAFF KGYPSFYYPA TLVAPVHSAV TSSIMYKVQF DDATMSTVNS NQIKRFFLKK
GDVVQSTRLG KIKHTVVKTF RSTNEQLSLI AVDALNNDMV ILAHGEIEVT VPISTIYVAP
VNIRRFQGRD LSFSTLKDMK FEETSFLPSH DSQRNRSSLK ERDSSFVKKN LDSESNQLIF
DDCVFAFSGP VHEDAYDRSA LETVVQDHGG LVLDTGLRPL FNDPFKSKQK KLRHLKPQKR
SKSWNQAFVV SDTFSRKVKY LEALAFNIPC VHPQFIKQCL KMNRVVDFSP YLLASGYSHR
LDCTLSQRIE PFDTTDSLYD RLLARKGPLF GKKILFIIPE AKSWQKKIEN TEQGQKALAH
VYHALALGAD VEIRPNVAHL ECDLILTMDG NIVDETNCPV VDPEWIVECL ISQSDIST
