PKNG_MYCTU
ID PKNG_MYCTU Reviewed; 750 AA.
AC P9WI73; L0T3M0; P65728; P96256;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Serine/threonine-protein kinase PknG;
DE EC=2.7.11.1;
GN Name=pknG; OrderedLocusNames=Rv0410c; ORFNames=MTCY22G10.06c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15186418; DOI=10.1111/j.1365-2958.2004.04085.x;
RA Cowley S., Ko M., Pick N., Chow R., Downing K.J., Gordhan B.G., Betts J.C.,
RA Mizrahi V., Smith D.A., Stokes R.W., Av-Gay Y.;
RT "The Mycobacterium tuberculosis protein serine/threonine kinase PknG is
RT linked to cellular glutamate/glutamine levels and is important for growth
RT in vivo.";
RL Mol. Microbiol. 52:1691-1702(2004).
RN [3]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND
RP MUTAGENESIS OF LYS-181.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11496007; DOI=10.1099/00221287-147-8-2307;
RA Koul A., Choidas A., Tyagi A.K., Drlica K., Singh Y., Ullrich A.;
RT "Serine/threonine protein kinases PknF and PknG of Mycobacterium
RT tuberculosis: characterization and localization.";
RL Microbiology 147:2307-2314(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH GARA,
RP AND AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL Mol. Microbiol. 70:1408-1423(2008).
RN [5]
RP FUNCTION IN ANTIBIOTIC RESISTANCE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19528288; DOI=10.1128/aac.00012-09;
RA Wolff K.A., Nguyen H.T., Cartabuke R.H., Singh A., Ogwang S., Nguyen L.;
RT "Protein kinase G is required for intrinsic antibiotic resistance in
RT mycobacteria.";
RL Antimicrob. Agents Chemother. 53:3515-3519(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, DOMAIN, PHOSPHORYLATION AT THR-63, AND MUTAGENESIS OF THR-63;
RP CYS-106; CYS-109; CYS-128; CYS-131; LYS-181 AND THR-309.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19638631; DOI=10.1074/jbc.m109.036095;
RA Tiwari D., Singh R.K., Goswami K., Verma S.K., Prakash B., Nandicoori V.K.;
RT "Key residues in Mycobacterium tuberculosis protein kinase G play a role in
RT regulating kinase activity and survival in the host.";
RL J. Biol. Chem. 284:27467-27479(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 74-750 IN COMPLEX WITH INHIBITOR
RP AX20017, FUNCTION, ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP ILE-87; ALA-92; CYS-106; CYS-109; CYS-128 AND CYS-131.
RX PubMed=17616581; DOI=10.1073/pnas.0702842104;
RA Scherr N., Honnappa S., Kunz G., Mueller P., Jayachandran R., Winkler F.,
RA Pieters J., Steinmetz M.O.;
RT "Structural basis for the specific inhibition of protein kinase G, a
RT virulence factor of Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12151-12156(2007).
CC -!- FUNCTION: Phosphorylates GarA. May play a role in metabolic regulation
CC via control of the phosphorylation status of GarA. Plays a crucial role
CC in the survival of mycobacteria within host macrophages, by blocking
CC the intracellular degradation of mycobacteria in lysosomes. Required
CC for intrinsic antibiotic resistance. {ECO:0000269|PubMed:17616581,
CC ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19528288,
CC ECO:0000269|PubMed:19638631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11496007, ECO:0000269|PubMed:15186418,
CC ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19638631};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11496007,
CC ECO:0000269|PubMed:15186418, ECO:0000269|PubMed:19019160,
CC ECO:0000269|PubMed:19638631};
CC -!- ACTIVITY REGULATION: Kinase activity is regulated by the redox status
CC of the environment via the rubredoxin domain. Autophosphorylation is
CC not essential for kinase activity, but it promotes binding to GarA. The
CC C-terminal domain also contributes to the regulation of activity.
CC Inhibited by a specific small molecular-weight inhibitor, the
CC tetrahydrobenzothiophene AX20017. {ECO:0000269|PubMed:17616581,
CC ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19638631}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2122 nM for GarA {ECO:0000269|PubMed:19638631};
CC -!- SUBUNIT: Homodimer. Interacts with the FHA domain of GarA.
CC {ECO:0000269|PubMed:17616581, ECO:0000269|PubMed:19019160}.
CC -!- INTERACTION:
CC P9WI73; P9WJA9: garA; NbExp=6; IntAct=EBI-6405537, EBI-6405522;
CC P9WI73; P9WI73: pknG; NbExp=4; IntAct=EBI-6405537, EBI-6405537;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Also detected in
CC growth media, suggesting that it can be translocated into host
CC macrophages under specific conditions.
CC -!- DOMAIN: Contains an N-terminal rubredoxin domain, a central kinase
CC domain and a C-terminal TPR domain. {ECO:0000269|PubMed:17616581,
CC ECO:0000269|PubMed:19638631}.
CC -!- PTM: Autophosphorylated. In vitro, incorporates up to four phosphate
CC groups on Thr-23, Thr-32 and Thr-63 and/or Thr-64 and/or Ser-65. In
CC vivo, is probably phosphorylated only on Thr-63.
CC {ECO:0000269|PubMed:19638631}.
CC -!- DISRUPTION PHENOTYPE: Disruption causes delayed mortality in mice.
CC Mutant accumulates glutamate and glutamine.
CC {ECO:0000269|PubMed:15186418}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL123456; CCP43141.1; -; Genomic_DNA.
DR PIR; H70628; H70628.
DR RefSeq; NP_214924.1; NC_000962.3.
DR RefSeq; WP_003402100.1; NZ_NVQJ01000002.1.
DR PDB; 2PZI; X-ray; 2.40 A; A/B=74-750.
DR PDB; 4Y0X; X-ray; 1.74 A; A=74-405.
DR PDB; 4Y12; X-ray; 1.90 A; A=74-405.
DR PDBsum; 2PZI; -.
DR PDBsum; 4Y0X; -.
DR PDBsum; 4Y12; -.
DR AlphaFoldDB; P9WI73; -.
DR SMR; P9WI73; -.
DR IntAct; P9WI73; 1.
DR STRING; 83332.Rv0410c; -.
DR ChEMBL; CHEMBL6070; -.
DR DrugBank; DB07398; 2-[(CYCLOPROPYLCARBONYL)AMINO]-4,5,6,7-TETRAHYDRO-1-BENZOTHIOPHENE-3-CARBOXAMIDE.
DR iPTMnet; P9WI73; -.
DR PaxDb; P9WI73; -.
DR DNASU; 886397; -.
DR GeneID; 886397; -.
DR KEGG; mtu:Rv0410c; -.
DR TubercuList; Rv0410c; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; PHCGSAY; -.
DR PhylomeDB; P9WI73; -.
DR BRENDA; 2.7.11.1; 3445.
DR SABIO-RK; P9WI73; -.
DR PRO; PR:P9WI73; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MTBBASE.
DR GO; GO:0006538; P:glutamate catabolic process; IMP:MTBBASE.
DR GO; GO:0006543; P:glutamine catabolic process; IMP:MTBBASE.
DR GO; GO:0052064; P:induction by symbiont of defense-related host reactive oxygen species production; IMP:MTBBASE.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:MTBBASE.
DR GO; GO:0052027; P:modulation by symbiont of host signal transduction pathway; IMP:MTBBASE.
DR GO; GO:0001899; P:negative regulation of cytolysis by symbiont of host cells; IMP:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR DisProt; DP01153; -.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031634; PknG_rubred.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16919; PknG_rubred; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW TPR repeat; Transferase; Virulence.
FT CHAIN 1..750
FT /note="Serine/threonine-protein kinase PknG"
FT /id="PRO_0000171216"
FT DOMAIN 151..396
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 536..569
FT /note="TPR"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 157..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 63
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19638631"
FT MUTAGEN 63
FT /note="T->A: Lack of phosphorylation. Does not affect
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:19638631"
FT MUTAGEN 87
FT /note="I->S: Decreases inhibition by AX20017; when
FT associated with S-92."
FT /evidence="ECO:0000269|PubMed:17616581"
FT MUTAGEN 92
FT /note="A->S: Decreases inhibition by AX20017; when
FT associated with S-87."
FT /evidence="ECO:0000269|PubMed:17616581"
FT MUTAGEN 106
FT /note="C->A: Decrease in activity; when associated with A-
FT 109; A-128 and A-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 106
FT /note="C->S: Lack of activity; when associated with S-109;
FT S-128 and S-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 109
FT /note="C->A: Decrease in activity; when associated with A-
FT 106; A-128 and A-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 109
FT /note="C->S: Lack of activity; when associated with S-106;
FT S-128 and S-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 128
FT /note="C->A: Decrease in activity; when associated with A-
FT 106; A-109 and A-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 128
FT /note="C->S: Lack of activity; when associated with S-106;
FT S-109 and S-131."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 131
FT /note="C->A: Decrease in activity; when associated with A-
FT 106; A-109 and A-128."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 131
FT /note="C->S: Lack of activity; when associated with S-106;
FT S-109 and S-128."
FT /evidence="ECO:0000269|PubMed:17616581,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 181
FT /note="K->M: Lack of activity."
FT /evidence="ECO:0000269|PubMed:11496007,
FT ECO:0000269|PubMed:19638631"
FT MUTAGEN 309
FT /note="T->A,D,E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:19638631"
FT MUTAGEN 309
FT /note="T->S: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19638631"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2PZI"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4Y0X"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4Y0X"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4Y0X"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:4Y0X"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 250..269
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4Y0X"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:4Y0X"
FT HELIX 385..403
FT /evidence="ECO:0007829|PDB:4Y0X"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2PZI"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:2PZI"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 503..515
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 518..532
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 536..549
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 552..565
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 571..583
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 636..646
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 658..669
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 678..693
FT /evidence="ECO:0007829|PDB:2PZI"
FT STRAND 699..703
FT /evidence="ECO:0007829|PDB:2PZI"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 710..727
FT /evidence="ECO:0007829|PDB:2PZI"
FT HELIX 731..744
FT /evidence="ECO:0007829|PDB:2PZI"
SQ SEQUENCE 750 AA; 81577 MW; CFC6E54DBE19569F CRC64;
MAKASETERS GPGTQPADAQ TATSATVRPL STQAVFRPDF GDEDNFPHPT LGPDTEPQDR
MATTSRVRPP VRRLGGGLVE IPRAPDIDPL EALMTNPVVP ESKRFCWNCG RPVGRSDSET
KGASEGWCPY CGSPYSFLPQ LNPGDIVAGQ YEVKGCIAHG GLGWIYLALD RNVNGRPVVL
KGLVHSGDAE AQAMAMAERQ FLAEVVHPSI VQIFNFVEHT DRHGDPVGYI VMEYVGGQSL
KRSKGQKLPV AEAIAYLLEI LPALSYLHSI GLVYNDLKPE NIMLTEEQLK LIDLGAVSRI
NSFGYLYGTP GFQAPEIVRT GPTVATDIYT VGRTLAALTL DLPTRNGRYV DGLPEDDPVL
KTYDSYGRLL RRAIDPDPRQ RFTTAEEMSA QLTGVLREVV AQDTGVPRPG LSTIFSPSRS
TFGVDLLVAH TDVYLDGQVH AEKLTANEIV TALSVPLVDP TDVAASVLQA TVLSQPVQTL
DSLRAARHGA LDADGVDFSE SVELPLMEVR ALLDLGDVAK ATRKLDDLAE RVGWRWRLVW
YRAVAELLTG DYDSATKHFT EVLDTFPGEL APKLALAATA ELAGNTDEHK FYQTVWSTND
GVISAAFGLA RARSAEGDRV GAVRTLDEVP PTSRHFTTAR LTSAVTLLSG RSTSEVTEEQ
IRDAARRVEA LPPTEPRVLQ IRALVLGGAL DWLKDNKAST NHILGFPFTS HGLRLGVEAS
LRSLARVAPT QRHRYTLVDM ANKVRPTSTF
