DPO1_GEOSE
ID DPO1_GEOSE Reviewed; 876 AA.
AC P52026;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; Synonyms=pol;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7557480; DOI=10.1016/0378-1119(95)00387-l;
RA Phang S.M., Teo C.Y., Lo E., Wong V.W.;
RT "Cloning and complete sequence of the DNA polymerase-encoding gene
RT (BstpolI) and characterisation of the Klenow-like fragment from Bacillus
RT stearothermophilus.";
RL Gene 163:65-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5 AND 289-293,
RP CHARACTERIZATION, AND MUTAGENESIS TO REMOVE 5'-3' EXONUCLEASE ACTIVITY.
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RX PubMed=8679703; DOI=10.1016/0167-4781(96)00051-6;
RA Riggs M.G., Tudor S., Sivaram M., McDonough S.H.;
RT "Construction of single amino acid substitution mutants of cloned Bacillus
RT stearothermophilus DNA polymerase I which lack 5'-3' exonuclease
RT activity.";
RL Biochim. Biophys. Acta 1307:178-186(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 297-876.
RC STRAIN=X;
RX PubMed=9016716; DOI=10.1016/s0969-2126(97)00169-x;
RA Kiefer J.R., Mao C., Hansen C.J., Basehore S.L., Hogrefe H.H., Braman J.C.,
RA Beese L.S.;
RT "Crystal structure of a thermostable Bacillus DNA polymerase I large
RT fragment at 2.1-A resolution.";
RL Structure 5:95-108(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 297-876.
RC STRAIN=X;
RX PubMed=9440698; DOI=10.1038/34693;
RA Kiefer J.R., Mao C., Braman J.C., Beese L.S.;
RT "Visualizing DNA replication in a catalytically active Bacillus DNA
RT polymerase crystal.";
RL Nature 391:304-307(1998).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.;
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC -!- MISCELLANEOUS: The enzyme from this organism does not have any 3'-5'
CC exonuclease activity. The subtilisin large fragment (residues 289-876)
CC has wild-type polymerase activity but no 5'-3' exonuclease activity.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- CAUTION: PubMed:9016716 and PubMed:9440698 strain is not known and has
CC been termed 'X' in this entry. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U23149; AAA85558.1; ALT_INIT; Genomic_DNA.
DR EMBL; L42111; AAC37139.1; -; Genomic_DNA.
DR PIR; JC4286; JC4286.
DR PIR; S70368; S70368.
DR PDB; 1L3S; X-ray; 1.70 A; A=301-876.
DR PDB; 1L3T; X-ray; 1.70 A; A=301-876.
DR PDB; 1L3U; X-ray; 1.80 A; A=301-876.
DR PDB; 1L3V; X-ray; 1.71 A; A=301-876.
DR PDB; 1L5U; X-ray; 1.95 A; A=301-876.
DR PDB; 1LV5; X-ray; 1.95 A; A/B=301-876.
DR PDB; 1NJX; X-ray; 1.65 A; A=301-876.
DR PDB; 1NJY; X-ray; 2.00 A; A=301-876.
DR PDB; 1NJZ; X-ray; 2.00 A; A=301-876.
DR PDB; 1NK0; X-ray; 1.70 A; A=301-876.
DR PDB; 1NK4; X-ray; 1.60 A; A=301-876.
DR PDB; 1NK5; X-ray; 2.10 A; A=301-876.
DR PDB; 1NK6; X-ray; 2.10 A; A=301-876.
DR PDB; 1NK7; X-ray; 1.90 A; A=301-876.
DR PDB; 1NK8; X-ray; 1.90 A; A=301-876.
DR PDB; 1NK9; X-ray; 1.90 A; A=301-876.
DR PDB; 1NKB; X-ray; 2.00 A; A=301-876.
DR PDB; 1NKC; X-ray; 1.80 A; A=301-876.
DR PDB; 1NKE; X-ray; 1.80 A; A=301-876.
DR PDB; 1U45; X-ray; 2.01 A; A=301-876.
DR PDB; 1U47; X-ray; 2.00 A; A=301-876.
DR PDB; 1U48; X-ray; 2.10 A; A=301-876.
DR PDB; 1U49; X-ray; 2.15 A; A=301-876.
DR PDB; 1U4B; X-ray; 1.60 A; A=301-876.
DR PDB; 1UA1; X-ray; 2.00 A; A=301-876.
DR PDB; 1XC9; X-ray; 1.90 A; A=301-876.
DR PDB; 1XWL; X-ray; 1.70 A; A=297-876.
DR PDB; 2BDP; X-ray; 1.80 A; A=297-876.
DR PDB; 3BDP; X-ray; 1.90 A; A=297-876.
DR PDB; 3EYZ; X-ray; 2.10 A; A=304-876.
DR PDB; 3EZ5; X-ray; 1.90 A; A/D=304-876.
DR PDB; 4BDP; X-ray; 1.80 A; A=297-876.
DR PDBsum; 1L3S; -.
DR PDBsum; 1L3T; -.
DR PDBsum; 1L3U; -.
DR PDBsum; 1L3V; -.
DR PDBsum; 1L5U; -.
DR PDBsum; 1LV5; -.
DR PDBsum; 1NJX; -.
DR PDBsum; 1NJY; -.
DR PDBsum; 1NJZ; -.
DR PDBsum; 1NK0; -.
DR PDBsum; 1NK4; -.
DR PDBsum; 1NK5; -.
DR PDBsum; 1NK6; -.
DR PDBsum; 1NK7; -.
DR PDBsum; 1NK8; -.
DR PDBsum; 1NK9; -.
DR PDBsum; 1NKB; -.
DR PDBsum; 1NKC; -.
DR PDBsum; 1NKE; -.
DR PDBsum; 1U45; -.
DR PDBsum; 1U47; -.
DR PDBsum; 1U48; -.
DR PDBsum; 1U49; -.
DR PDBsum; 1U4B; -.
DR PDBsum; 1UA1; -.
DR PDBsum; 1XC9; -.
DR PDBsum; 1XWL; -.
DR PDBsum; 2BDP; -.
DR PDBsum; 3BDP; -.
DR PDBsum; 3EYZ; -.
DR PDBsum; 3EZ5; -.
DR PDBsum; 4BDP; -.
DR AlphaFoldDB; P52026; -.
DR SMR; P52026; -.
DR DrugBank; DB07435; 1,2,3-TRIHYDROXY-1,2,3,4-TETRAHYDROBENZO[A]PYRENE.
DR BRENDA; 2.7.7.7; 623.
DR EvolutionaryTrace; P52026; -.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 2.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Transferase.
FT CHAIN 1..876
FT /note="DNA polymerase I"
FT /id="PRO_0000101234"
FT DOMAIN 1..310
FT /note="5'-3' exonuclease"
FT REGION 289..876
FT /note="Subtilisin large fragment"
FT REGION 469..876
FT /note="Polymerase"
FT VARIANT 298
FT /note="G -> K (in strain: X)"
FT VARIANT 300
FT /note="D -> A (in strain: X)"
FT VARIANT 302..303
FT /note="AI -> TL (in strain: X)"
FT VARIANT 306
FT /note="S -> R (in strain: X)"
FT VARIANT 309
FT /note="D -> E (in strain: X)"
FT VARIANT 320
FT /note="V -> L (in strain: X)"
FT VARIANT 324..325
FT /note="GD -> EE (in strain: X)"
FT VARIANT 329
FT /note="H -> D (in strain: X)"
FT VARIANT 337..338
FT /note="LA -> VV (in strain: X)"
FT VARIANT 341
FT /note="R -> H (in strain: X)"
FT VARIANT 356
FT /note="K -> Q (in strain: X)"
FT VARIANT 358
FT /note="L -> V (in strain: X)"
FT VARIANT 369
FT /note="T -> S (in strain: X)"
FT VARIANT 388
FT /note="R -> C (in strain: X)"
FT VARIANT 391
FT /note="V -> S (in strain: X)"
FT VARIANT 406..408
FT /note="AAG -> GVD (in strain: X)"
FT VARIANT 411
FT /note="A -> R (in strain: X)"
FT VARIANT 413
FT /note="V -> A (in strain: X)"
FT VARIANT 417
FT /note="H -> K (in strain: X)"
FT VARIANT 424
FT /note="S -> P (in strain: X)"
FT VARIANT 436
FT /note="T -> A (in strain: X)"
FT VARIANT 442
FT /note="T -> V (in strain: X)"
FT VARIANT 456
FT /note="A -> E (in strain: X)"
FT VARIANT 459
FT /note="E -> R (in strain: X)"
FT VARIANT 461..462
FT /note="LM -> FL (in strain: X)"
FT VARIANT 475
FT /note="T -> V (in strain: X)"
FT VARIANT 482..483
FT /note="AG -> SS (in strain: X)"
FT VARIANT 487
FT /note="N -> E (in strain: X)"
FT VARIANT 491
FT /note="T -> A (in strain: X)"
FT VARIANT 505
FT /note="A -> K (in strain: X)"
FT VARIANT 508
FT /note="T -> R (in strain: X)"
FT VARIANT 510
FT /note="Q -> K (in strain: X)"
FT VARIANT 512..513
FT /note="QA -> GT (in strain: X)"
FT VARIANT 516
FT /note="R -> Q (in strain: X)"
FT VARIANT 536..537
FT /note="TV -> VI (in strain: X)"
FT VARIANT 540
FT /note="D -> E (in strain: X)"
FT VARIANT 567
FT /note="H -> Y (in strain: X)"
FT VARIANT 573
FT /note="H -> N (in strain: X)"
FT VARIANT 596
FT /note="H -> R (in strain: X)"
FT VARIANT 598
FT /note="V -> D (in strain: X)"
FT VARIANT 600
FT /note="G -> K (in strain: X)"
FT VARIANT 605
FT /note="M -> I (in strain: X)"
FT VARIANT 619
FT /note="V -> T (in strain: X)"
FT VARIANT 645
FT /note="P -> S (in strain: X)"
FT VARIANT 672
FT /note="I -> M (in strain: X)"
FT VARIANT 678
FT /note="G -> D (in strain: X)"
FT VARIANT 691
FT /note="H -> Q (in strain: X)"
FT VARIANT 695..696
FT /note="ED -> DE (in strain: X)"
FT VARIANT 699
FT /note="A -> P (in strain: X)"
FT VARIANT 728
FT /note="T -> S (in strain: X)"
FT VARIANT 741
FT /note="A -> E (in strain: X)"
FT VARIANT 748
FT /note="Q -> R (in strain: X)"
FT VARIANT 751
FT /note="D -> E (in strain: X)"
FT VARIANT 790
FT /note="T -> M (in strain: X)"
FT VARIANT 812..813
FT /note="SV -> NA (in strain: X)"
FT VARIANT 816
FT /note="R -> K (in strain: X)"
FT VARIANT 841
FT /note="I -> M (in strain: X)"
FT VARIANT 870
FT /note="P -> S (in strain: X)"
FT MUTAGEN 73
FT /note="Y->A,P: Complete loss of 5'-3' exonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:8679703"
FT CONFLICT 91
FT /note="L -> V (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="E -> K (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="L -> V (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 381..382
FT /note="KW -> NG (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="R -> AGV (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="H -> Q (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="V -> A (in Ref. 1; AAC37139)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..480
FT /note="QP -> HA (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="G -> W (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="S -> T (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..815
FT /note="RL -> SV (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="V -> G (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="E -> G (in Ref. 2; AAA85558)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="T -> A (in Ref. 1; AAC37139)"
FT /evidence="ECO:0000305"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1U4B"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:1NK4"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:1NK4"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 440..467
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 497..522
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:2BDP"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 558..564
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 570..587
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 589..594
FT /evidence="ECO:0007829|PDB:1NK4"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:1XWL"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:1XWL"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 635..639
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 647..656
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 657..666
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 669..676
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 694..696
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 699..714
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 718..725
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 729..742
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 744..760
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 774..777
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 781..817
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 823..827
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 829..837
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 838..840
FT /evidence="ECO:0007829|PDB:1NK4"
FT HELIX 841..853
FT /evidence="ECO:0007829|PDB:1NK4"
FT STRAND 864..871
FT /evidence="ECO:0007829|PDB:1NK4"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:1NK4"
SQ SEQUENCE 876 AA; 98670 MW; 689167A801D543E4 CRC64;
MKNKLVLIDG NSVAYRAFFA LPLLHNDKGI HTNAVYGFTM MLNKILAEEQ PTHILVAFDA
GKTTFRHETF QDYKGGRQQT PPELSEQFPL LRELLKAYRI PAYELDHYEA DDIIGTMAAR
AEREGFAVKV ISGDRDLTQL ASPQVTVEIT KKGITDIESY TPETVVEKYG LTPEQIVDLK
GLMGDKSDNI PGVPGIGEKT AVKLLKQFGT VENVLASIDE IKGEKLKENL RQYRDLALLS
KQLAAICRDA PVELTLDDIV YKGEDREKVV ALFQELGFQS FLDKMAVQTD EGEKPLAGMD
FAIADSVTDE MLADKAALVV EVVGDNYHHA PIVGIALANE RGRFFLRPET ALADPKFLAW
LGDETKKKTM FDSKRAAVAL KWKGIELRGV VFDLLLAAYL LDPAQAAGDV AAVAKMHQYE
AVRSDEAVYG KGAKRTVPDE PTLAEHLVRK AAAIWALEEP LMDELRRNEQ DRLLTELEQP
LAGILANMEF TGVKVDTKRL EQMGAELTEQ LQAVERRIYE LAGQEFNINS PKQLGTVLFD
KLQLPVLKKT KTGYSTSADV LEKLAPHHEI VEHILHYRQL GKLQSTYIEG LLKVVHPVTG
KVHTMFNQAL TQTGRLSSVE PNLQNIPIRL EEGRKIRQAF VPSEPDWLIF AADYSQIELR
VLAHIAEDDN LIEAFRRGLD IHTKTAMDIF HVSEEDVTAN MRRQAKAVNF GIVYGISDYG
LAQNLNITRK EAAEFIERYF ASFPGVKQYM DNIVQEAKQK GYVTTLLHRR RYLPDITSRN
FNVRSFAERT AMNTPIQGSA ADIIKKAMID LSVRLREERL QARLLLQVHD ELILEAPKEE
IERLCRLVPE VMEQAVTLRV PLKVDYHYGP TWYDAK
