NTPES_BACSU
ID NTPES_BACSU Reviewed; 1462 AA.
AC O34313; Q79EX6;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Trifunctional nucleotide phosphoesterase protein YfkN;
DE Includes:
DE RecName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
DE EC=3.1.3.6;
DE EC=3.1.4.16;
DE Includes:
DE RecName: Full=5'-nucleotidase;
DE EC=3.1.3.5;
DE Flags: Precursor;
GN Name=yfkN; OrderedLocusNames=BSU07840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 36-43 AND 955-960, FUNCTION AS A TRIFUNCTIONAL
RP NUCLEOTIDE PHOSPHOESTERASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP SUBSTRATE SPECIFICITY, DOMAIN N-TERMINAL, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=14688230; DOI=10.1093/jb/mvg189;
RA Chambert R., Pereira Y., Petit-Glatron M.-F.;
RT "Purification and characterization of yfkN, a trifunctional nucleotide
RT phosphoesterase secreted by Bacillus subtilis.";
RL J. Biochem. 134:655-660(2003).
RN [4]
RP INDUCTION BY PHOSPHATE STARVATION.
RC STRAIN=168;
RX PubMed=16291680; DOI=10.1128/jb.187.23.8063-8080.2005;
RA Allenby N.E.E., O'Connor N., Pragai Z., Ward A.C., Wipat A., Harwood C.R.;
RT "Genome-wide transcriptional analysis of the phosphate starvation stimulon
RT of Bacillus subtilis.";
RL J. Bacteriol. 187:8063-8080(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE D.
RX PubMed=21906378; DOI=10.1186/2191-0855-1-22;
RA Nguyen H.D., Phan T.T., Schumann W.;
RT "Analysis and application of Bacillus subtilis sortases to anchor
RT recombinant proteins on the cell wall.";
RL AMB Express 1:22-22(2011).
RN [6]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE D.
RX PubMed=21800427; DOI=10.1002/pmic.201100174;
RA Fasehee H., Westers H., Bolhuis A., Antelmann H., Hecker M., Quax W.J.,
RA Mirlohi A.F., van Dijl J.M., Ahmadian G.;
RT "Functional analysis of the sortase YhcS in Bacillus subtilis.";
RL Proteomics 11:3905-3913(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 37-374 IN COMPLEX WITH DIVALENT
RP METAL CATIONS.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of calcineurin-like phosphoesterase from Bacillus
RT subtilis.";
RL Submitted (APR-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the release of inorganic phosphate from 2',3'-
CC cyclic nucleotides through consecutive 2',3'-phosphodiesterase and
CC 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase
CC activity. Does not catalyze the release of inorganic phosphate from
CC 3',5'-cyclic nucleotides. Probably plays a role in the cellular
CC reprocessing of nucleotides present in the medium, under conditions of
CC phosphate shortage. {ECO:0000269|PubMed:14688230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000269|PubMed:14688230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000269|PubMed:14688230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000269|PubMed:14688230};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=The 2',3'-cyclic phosphodiesterase activity is higher than that
CC of the 5'-nucleotidase with the four major nucleotides used as
CC substrates. {ECO:0000269|PubMed:14688230};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:21800427,
CC ECO:0000269|PubMed:21906378, ECO:0000305|PubMed:14688230};
CC Peptidoglycan-anchor {ECO:0000305|PubMed:14688230}. Note=Anchored to
CC the cell wall by sortase SrtD. {ECO:0000269|PubMed:21800427,
CC ECO:0000269|PubMed:21906378}.
CC -!- INDUCTION: Expression is induced in response to phosphate starvation in
CC a PhoR-dependent manner. {ECO:0000269|PubMed:16291680}.
CC -!- DOMAIN: The N-terminal region (amino acids 35-623) is able to catalyze
CC the release of phosphate from 2',3'-cyclic nucleotides, but not from
CC 5'-nucleotides. {ECO:0000269|PubMed:14688230}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; D83967; BAA23404.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12613.1; -; Genomic_DNA.
DR PIR; A69809; A69809.
DR RefSeq; NP_388665.1; NC_000964.3.
DR RefSeq; WP_010886443.1; NZ_JNCM01000032.1.
DR PDB; 3GVE; X-ray; 1.25 A; A/B=37-374.
DR PDBsum; 3GVE; -.
DR AlphaFoldDB; O34313; -.
DR SMR; O34313; -.
DR IntAct; O34313; 1.
DR STRING; 224308.BSU07840; -.
DR PaxDb; O34313; -.
DR PRIDE; O34313; -.
DR DNASU; 936131; -.
DR EnsemblBacteria; CAB12613; CAB12613; BSU_07840.
DR GeneID; 936131; -.
DR KEGG; bsu:BSU07840; -.
DR PATRIC; fig|224308.43.peg.822; -.
DR eggNOG; COG0737; Bacteria.
DR InParanoid; O34313; -.
DR OMA; DAQKWYA; -.
DR BioCyc; BSUB:BSU07840-MON; -.
DR EvolutionaryTrace; O34313; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IBA:GO_Central.
DR CDD; cd07410; MPP_CpdB_N; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR Gene3D; 3.90.780.10; -; 2.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR041827; CpdB_N.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 2.
DR Pfam; PF02872; 5_nucleotid_C; 2.
DR Pfam; PF00149; Metallophos; 2.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 2.
DR SUPFAM; SSF56300; SSF56300; 2.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 2.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Peptidoglycan-anchor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:14688230"
FT CHAIN 36..1427
FT /note="Trifunctional nucleotide phosphoesterase protein
FT YfkN"
FT /id="PRO_0000390884"
FT PROPEP 1428..1462
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000390885"
FT REGION 36..623
FT /note="2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-
FT nucleotidase"
FT REGION 624..1427
FT /note="5'-nucleotidase"
FT REGION 1350..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1424..1428
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1389..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 54
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT BINDING 282
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT BINDING 284
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 458
FT /ligand="a ribonucleoside 3'-phosphate"
FT /ligand_id="ChEBI:CHEBI:13197"
FT /evidence="ECO:0000250"
FT BINDING 561..567
FT /ligand="a ribonucleoside 3'-phosphate"
FT /ligand_id="ChEBI:CHEBI:13197"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 740
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 872
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 895
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 897
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1047
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000250"
FT BINDING 1127..1133
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000250"
FT MOD_RES 1427
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3GVE"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:3GVE"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3GVE"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 318..330
FT /evidence="ECO:0007829|PDB:3GVE"
FT STRAND 333..346
FT /evidence="ECO:0007829|PDB:3GVE"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:3GVE"
FT HELIX 355..373
FT /evidence="ECO:0007829|PDB:3GVE"
SQ SEQUENCE 1462 AA; 159706 MW; EE769201F34DA84C CRC64;
MRIQKRRTHV ENILRILLPP IMILSLILPT PPIHAEESAA PQVHLSILAT TDIHANMMDY
DYYSDKETAD FGLARTAQLI QKHREQNPNT LLVDNGDLIQ GNPLGEYAVK YQKDDIISGT
KTHPIISVMN ALKYDAGTLG NHEFNYGLDF LDGTIKGADF PIVNANVKTT SGENRYTPYV
INEKTLIDEN GNEQKVKVGY IGFVPPQIMT WDKKNLEGQV QVQDIVESAN ETIPKMKAEG
ADVIIALAHT GIEKQAQSSG AENAVFDLAT KTKGIDAIIS GHQHGLFPSA EYAGVAQFNV
EKGTINGIPV VMPSSWGKYL GVIDLKLEKA DGSWKVADSK GSIESIAGNV TSRNETVTNT
IQQTHQNTLE YVRKPVGKTE ADINSFFAQV KDDPSIQIVT DAQKWYAEKE MKDTEYKNLP
ILSAGAPFKA GGRNGANYYT NIPAGDLAIK NVGDLYLYDN TVQIVKLTGS EVKDWLEMSA
GQFNQIDPAK GGDQALLNEN FRSYNFDVID GVTYQVDVTK PAKYNENGKV INADSSRIIN
LSYEGKPISP SQEFLVVTNN YRASGGGGFP HLTSDKIVHG SAVENRQVLM DYIIEQKTVN
PKADNNWSIA PVSGTNLTFE SSLLAKPFAD KADDVAYVGK SANEGYGVYK LQFDDDSNPD
PPKDGLWDLT VMHTNDTHAH LDDAARRMTK INEVRSETNH NILLDAGDVF SGDLYFTKWN
GLADLKMMNM MGYDAMTFGN HEFDKGPTVL SDFLSGNSAT VDPANRYHFE APEFPIVSAN
VDVSNEPKLK SFVKKPQTFT AGEKKEAGIH PYILLDVDGE KVAVFGLTTE DTATTSSPGK
SIVFNDAFET AQNTVKAIQE EEKVNKIIAL THIGHNRDLE LAKKVKGIDL IIGGHTHTLV
DKMEVVNNEE PTIVAQAKEY GQFLGRVDVA FDEKGVVQTD KSNLSVLPID EHTEENPEAK
QELDQFKNEL EDVKNEKVGY TDVALDGQRE HVRTKETNLG NFIADGMLAK AKEAAGARIA
ITNGGGIRAG IDKGDITLGE VLNVMPFGNT LYVADLTGKQ IKEALEQGLS NVENGGGAFP
QVAGIEYTFT LNNKPGHRVL EVKIESPNGD KVAINTDDTY RVATNNFVGA GGDGYSVFTE
ASHGEDLGYV DYEIFTEQLK KLGNKVSPKV EGRIKEVFLP TKQKDGSWTL DEDKFAIYAK
NANTPFVYYG IHEGSQEKPI NLKVKKDQVK LLKERESDPS LTMFNYWYSM KMPMANLKTA
DTAIGIKSTG ELDVSLSDVY DFTVKQKGKE IKSFKEPVQL SLRMFDIEEA HNPAIYHVDR
KKKAFTKTGH GSVDDDMVTG YTNHFSEYTI LNSGSNNKPP AFPSDQPTGG DDGNHGGGSD
KPGGKQPTDG NGGNDTPPGT QPTNGSGGNG SGGSGTDGPA GGLLPDTATS MYSILLAGFL
ISALGTAMYL HQRRKQNRAN QA
