ID CHK1_CANAL Reviewed; 2471 AA.
AC Q5AHA0; A0A1D8PGV5; O59892;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Histidine protein kinase 1;
DE EC=2.7.13.3;
GN Name=CHK1; OrderedLocusNames=CAALFM_C203320WA;
GN ORFNames=CaO19.8515, CaO19.896;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=9639313;
RX DOI=10.1002/(sici)1097-0061(199805)14:7<665::aid-yea246>3.0.co;2-#;
RA Calera J.A., Choi G.H., Calderone R.A.;
RT "Identification of a putative histidine kinase two-component phosphorelay
RT gene (CaHK1) in Candida albicans.";
RL Yeast 14:665-674(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10411270; DOI=10.1099/13500872-145-6-1431;
RA Calera J.A., Calderone R.;
RT "Flocculation of hyphae is associated with a deletion in the putative CaHK1
RT two-component histidine kinase gene from Candida albicans.";
RL Microbiology 145:1431-1442(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10417206; DOI=10.1128/iai.67.8.4280-4284.1999;
RA Calera J.A., Zhao X.J., De Bernardis F., Sheridan M., Calderone R.;
RT "Avirulence of Candida albicans CaHK1 mutants in a murine model of
RT hematogenously disseminated candidiasis.";
RL Infect. Immun. 67:4280-4284(1999).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10572127; DOI=10.1128/jb.181.23.7243-7247.1999;
RA Yamada-Okabe T., Mio T., Ono N., Kashima Y., Matsui M., Arisawa M.,
RA Yamada-Okabe H.;
RT "Roles of three histidine kinase genes in hyphal development and virulence
RT of the pathogenic fungus Candida albicans.";
RL J. Bacteriol. 181:7243-7247(1999).
RN [8]
RP INDUCTION.
RX PubMed=11737641; DOI=10.1046/j.1365-2958.2001.02713.x;
RA Murad A.M., d'Enfert C., Gaillardin C., Tournu H., Tekaia F., Talibi D.,
RA Marechal D., Marchais V., Cottin J., Brown A.J.;
RT "Transcript profiling in Candida albicans reveals new cellular functions
RT for the transcriptional repressors CaTup1, CaMig1 and CaNrg1.";
RL Mol. Microbiol. 42:981-993(2001).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=11796636; DOI=10.1128/iai.70.2.985-987.2002;
RA Torosantucci A., Chiani P., De Bernardis F., Cassone A., Calera J.A.,
RA Calderone R.;
RT "Deletion of the two-component histidine kinase gene (CHK1) of Candida
RT albicans contributes to enhanced growth inhibition and killing by human
RT neutrophils in vitro.";
RL Infect. Immun. 70:985-987(2002).
RN [10]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=11854244; DOI=10.1128/iai.70.3.1558-1565.2002;
RA Li D., Bernhardt J., Calderone R.;
RT "Temporal expression of the Candida albicans genes CHK1 and CSSK1,
RT adherence, and morphogenesis in a model of reconstituted human esophageal
RT epithelial candidiasis.";
RL Infect. Immun. 70:1558-1565(2002).
RN [11]
RP FUNCTION.
RX PubMed=12689636; DOI=10.1111/j.1567-1364.2003.tb00170.x;
RA Kruppa M., Goins T., Cutler J.E., Lowman D., Williams D., Chauhan N.,
RA Menon V., Singh P., Li D., Calderone R.;
RT "The role of the Candida albicans histidine kinase (CHK1) gene in the
RT regulation of cell wall mannan and glucan biosynthesis.";
RL FEMS Yeast Res. 3:289-299(2003).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15302838; DOI=10.1128/ec.3.4.1062-1065.2004;
RA Kruppa M., Krom B.P., Chauhan N., Bambach A.V., Cihlar R.L.,
RA Calderone R.A.;
RT "The two-component signal transduction protein Chk1p regulates quorum
RT sensing in Candida albicans.";
RL Eukaryot. Cell 3:1062-1065(2004).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14734021; DOI=10.1016/s1567-1356(03)00201-0;
RA Kruppa M., Jabra-Rizk M.A., Meiller T.F., Calderone R.;
RT "The histidine kinases of Candida albicans: regulation of cell wall mannan
RT biosynthesis.";
RL FEMS Yeast Res. 4:409-416(2004).
RN [14]
RP INDUCTION.
RX PubMed=15470110; DOI=10.1099/mic.0.27237-0;
RA Li D., Gurkovska V., Sheridan M., Calderone R., Chauhan N.;
RT "Studies on the regulation of the two-component histidine kinase gene CHK1
RT in Candida albicans using the heterologous lacZ reporter gene.";
RL Microbiology 150:3305-3313(2004).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=17664325; DOI=10.1128/aac.00929-07;
RA Chauhan N., Kruppa M., Calderone R.;
RT "The Ssk1p response regulator and Chk1p histidine kinase mutants of Candida
RT albicans are hypersensitive to fluconazole and voriconazole.";
RL Antimicrob. Agents Chemother. 51:3747-3751(2007).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19563901; DOI=10.1016/j.fgb.2009.06.008;
RA Li D., Williams D., Lowman D., Monteiro M.A., Tan X., Kruppa M., Fonzi W.,
RA Roman E., Pla J., Calderone R.;
RT "The Candida albicans histidine kinase Chk1p: signaling and cell wall
RT mannan.";
RL Fungal Genet. Biol. 46:731-741(2009).
RN [17]
RP INDUCTION.
RX PubMed=20150241; DOI=10.1099/mic.0.037549-0;
RA Holcombe L.J., McAlester G., Munro C.A., Enjalbert B., Brown A.J.,
RA Gow N.A., Ding C., Butler G., O'Gara F., Morrissey J.P.;
RT "Pseudomonas aeruginosa secreted factors impair biofilm development in
RT Candida albicans.";
RL Microbiology 156:1476-1486(2010).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20688824; DOI=10.1099/mic.0.040006-0;
RA Klippel N., Cui S., Groebe L., Bilitewski U.;
RT "Deletion of the Candida albicans histidine kinase gene CHK1 improves
RT recognition by phagocytes through an increased exposure of cell wall beta-
RT 1,3-glucans.";
RL Microbiology 156:3432-3444(2010).
RN [19]
RP INDUCTION.
RX PubMed=23563485; DOI=10.1128/ec.00071-13;
RA Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
RT "Identification of genes upregulated by the transcription factor Bcr1 that
RT are involved in impermeability, impenetrability, and drug resistance of
RT Candida albicans a/alpha biofilms.";
RL Eukaryot. Cell 12:875-888(2013).
RN [20]
RP FUNCTION.
RX PubMed=23902848;
RA Su H.C., Cheng B.;
RT "Effects of histidine kinase gene CHK1 on some biological characteristics
RT of Candida albicans.";
RL Zhonghua Yi Xue Za Zhi 93:1109-1113(2013).
CC -!- FUNCTION: Histidine kinase involved in a two-component signaling
CC pathway that regulates cell wall mannan and glucan biosynthesis.
CC Regulates quorum sensing as well as hyphal formation, biofilm
CC formation, chlamidospore formation, and virulence. Plays a prominent
CC role in phagocyte activation. Involved in the covering of the most
CC potent pro-inflammatory cell wall molecules, the beta-glucans,
CC underneath a dense mannan layer, so that the pathogen becomes partly
CC invisible for immune cells such as phagocytes.
CC {ECO:0000269|PubMed:10417206, ECO:0000269|PubMed:10572127,
CC ECO:0000269|PubMed:12689636, ECO:0000269|PubMed:14734021,
CC ECO:0000269|PubMed:15302838, ECO:0000269|PubMed:19563901,
CC ECO:0000269|PubMed:20688824, ECO:0000269|PubMed:23902848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INDUCTION: Expression is detected as early as 1 hour after infection of
CC reconstituted human esophageal tissue and increases thereafter up to 48
CC hours postinfection. Expression is also increased when cells are
CC exposed to several types of stress. Expression is decreased by
CC Pseudomonas aeruginosa secretions. Moreover, expression is regulated by
CC NGR1 and BCR1. {ECO:0000269|PubMed:11737641,
CC ECO:0000269|PubMed:11854244, ECO:0000269|PubMed:15470110,
CC ECO:0000269|PubMed:20150241, ECO:0000269|PubMed:23563485}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from His-2007 (H1) in the histidine kinase domain
CC (transmitter domain) to Asp-2394 (D1) of the response regulatory domain
CC (receiver domain). This transfer probably occurs between two CHK1
CC molecules, rather than intramolecularly (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impairs the hyphal formation and attenuates the
CC virulence in a mouse systemic candidiasis model and towards
CC reconstituted human esophageal tissue. Leads to extensive flocculation
CC under conditions that stimulate germ-tube formation. Leads also to
CC increased growth-inhibitory and killing effect by human neutrophils
CC (polymorphonuclear leukocytes) and to hypersensitivity to fluconazole
CC and voriconazole. {ECO:0000269|PubMed:10411270,
CC ECO:0000269|PubMed:10417206, ECO:0000269|PubMed:10572127,
CC ECO:0000269|PubMed:11796636, ECO:0000269|PubMed:11854244,
CC ECO:0000269|PubMed:14734021, ECO:0000269|PubMed:15302838,
CC ECO:0000269|PubMed:17664325, ECO:0000269|PubMed:19563901,
CC ECO:0000269|PubMed:20688824}.
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DR EMBL; AF013273; AAC39451.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27368.1; -; Genomic_DNA.
DR RefSeq; XP_721017.2; XM_715924.2.
DR AlphaFoldDB; Q5AHA0; -.
DR SMR; Q5AHA0; -.
DR STRING; 237561.Q5AHA0; -.
DR EnsemblFungi; C2_03320W_A-T; C2_03320W_A-T-p1; C2_03320W_A.
DR GeneID; 3637394; -.
DR KEGG; cal:CAALFM_C203320WA; -.
DR CGD; CAL0000185875; CHK1.
DR VEuPathDB; FungiDB:C2_03320W_A; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000835_0_0_1; -.
DR InParanoid; Q5AHA0; -.
DR OrthoDB; 2734979at2759; -.
DR PHI-base; PHI:11569; -.
DR PHI-base; PHI:136; -.
DR PRO; PR:Q5AHA0; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0097308; P:cellular response to farnesol; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR GO; GO:0051042; P:negative regulation of calcium-independent cell-cell adhesion; IMP:CGD.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell wall biogenesis/degradation; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..2471
FT /note="Histidine protein kinase 1"
FT /id="PRO_0000425798"
FT DOMAIN 358..636
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 2004..2225
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 2340..2466
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2007
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 2394
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 2298
FT /note="V -> I (in Ref. 1; AAC39451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2471 AA; 281795 MW; 752618E1C1A10F80 CRC64;
MSMNFFNSSE PARDHKPDQE KETVMTTEHY EFERPDVKAI RNFKFFRSDE TETKKGPNLH
ISDLSPLESQ SVPPSALSLN HSIIPDQYER RQDTPDPIHT PEISLSDYLY DQTLSPQGFD
NSRENFNIHK TIASLFEDNS SVVSQESTDD TKTTLSSETC DSFSLNNASY LTNINFVQNH
LQYLSQNVLG NRTSNSLPPS SSSQIDFDAS NLTPDSIPGY ILNKKLGSVH QSTDSVYNAI
KIPQNEEYNC CTKASASQNP TNLNSKVIVR LSPNIFQNLS LSRFLNEWYI LSGKHSSKEH
QIWSNESLTN EYVQDKTIPT FDKESARFRP TLPINIPGIL YPQEIINFCV NSHDYPLEHP
SQSTDQKRFA MVYQDNDYKT FKELSMFTLH ELQTRQGSYS SNESRRKSSS GFNIGVNATT
TEAGSLESFS NLMQNHHLGA TSTNGDPFHS KLAKFEYGVS KSPMKLIEIL TDIMRVVETI
SVIHELGFVH NGLTSSNLLK SEKNVRDIKI TGWGFAFSFT ENCSQGYRNK HLAQVQDLIP
YMAPEVLAIT NSVVDYRSDF YSLGVIMYEL VLGILPFKNS NPQKLIRMHT FENPIAPSAL
APGWISEKLS GVIMKLLEKH PHNRYTDCHS LLHDLIEVKN MYISKLLDSG ETIPNSNLNL
SDRQYYLTKE NLLHPEKMGI TPVLGLKESF IGRRDFLQNV TEVYNNSKNG IDLLFISGES
GRGKTIILQD LRAAAVLKQD FYYSWKFSFF GADTHVYRFL VEGVQKIITQ ILNSSEEIQN
TWRDVILTHI PIDLSILFYL IPELKVLLGK KYTSIYKHKI GMGMLKRSFK EDQTSRLEIK
LRQILKEFFK LVAKQGLSIF LDDVQWCSEE SWRLLCDVLD FDSSGEVRES YNIKIVVCYA
LNADHLENVN IEHKKISFCR YAKQSHLNLR EFSIPHIPLE DAIEFLCEPY TRSHDHECNS
KKSDVIANLN CTNEYPQNTC KVIPSIIQEL YQSSEGNVLL LIFLTRMTKL SGKVPFQRFS
VKNSYLYDHL SNSNYGTTRK EILTNYLNMG TNSDTRALLK VAALISNGSG FFFSDLIVAT
DLPMAEAFQL LQICIHSRII VPTSTYYKIP MDLIASDQTP FDLTDDNIWK LATLCSYKFY
HDSICTHIIK ELNASGEFKE LSRLCGLRFY NTITKERLLN IGGYLQMATH FRNSYEVAGP
EENEKYVEVL VQAGRYAIST YNMKLSQWFF NVVGELVYNL DSKTQLKSVL TIAENHFNSR
EFEQCLSVVE NAQRKFGFDR LIFSIQIVRC KIELGDYDEA HRIAIECLKE LGVPLDDDDE
YTSENSLETC LGKIPLSVAD IRGILKIKRC KNSRTLLMYQ LISELIVLFK LQGKDKVRRF
LTAYAMSQIH TQGSSPYCAV ILIDFAQSFV NETTTSGMLK AKELSIVMLS LINRAPEISL
SYVQSIYEYY FSCHAVFFES IEKMSDLIHP GNASSHCTRS SYYSSFHLIV NVSKIFFSCM
NGESFKMFST FKCKSYLTGD PQMPEMDNFL YDSEMLLAGH SELNEFMRKY QSFNQTSVGK
FCYYLIVLLV MSREHRFDEA ADLVLKVLED LSEKLPVSFL HHQYYLICGK VFAYHQTKTP
ESEEQVERIL ARQFERYELW ASTNKPTLLP RYLLLSTYKQ IRENHVDKLE ILDSFEEALQ
TAHKFHNVYD MCWINLECAR WLISINQKRH RISRMVKQGL KILRSLELNN HLRLAEFEFD
EYIEDEDHRN KWAGLTNNPT LDTVTTWQQQ NMPDKVSPCN DKQLVHGKQF GKKEFDSHLL
RLHFDGQYTG LDLNSAIREC LAISEALDEN SILTKLMASA IKYSGATYGV IVTKKNQETP
FLRTIGSQHN IHTLNNMPIS DDICPAQLIR HVLHTGETVN KAHDHIGFAN KFENEYFQTT
DKKYSVVCLP LKSSLGLFGA LYLEGSDGDF GHEDLFNERK CDLLQLFCTQ AAVALGKERL
LLQMELAKMA AEDATDEKAS FLANMSHEIR TPFNSLLSFA IFLLDTKLDS TQREYVEAIQ
SSAMITLNII DGILAFSKIE HGSFTLENAP FSLNDCIETA IQVSGETILN DQIELVFCNN
CPEIEFVVGD LTRFRQIVIN LVGNAIKFTT KGHVLISCDS RKITDDRFEI NVSVEDSGIG
ISKKSQNKVF GAFSQVDGSA RREYGGSGLG LAISKKLTEL MGGTIRFESE EGIGTTFYVS
VIMDAKEYSS PPFSLNKKCL IYSQHCLTAK SISNMLNYFG STVKVTNQKS EFSTSVQAND
IIFVDRGMEP DVSCKTKVIP IDPKPFKRNK LISILKEQPS LPTKVFGNNK SNLSKQYPLR
ILLAEDNLLN YKVCLKHLDK LGYKADHAKD GVVVLDKCKE LLEKDEKYDV ILMDIQMPRK
DGITATRDLK TLFHTQKKES WLPVIVALTA NVAGDDKKRC LEEGMFDFIT KPILPDELRR
ILTKVGETVN M
//
