RPO2_SACSH
ID RPO2_SACSH Reviewed; 1131 AA.
AC B8YB55;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2 {ECO:0000303|PubMed:19419240};
DE EC=2.7.7.6 {ECO:0000305|PubMed:19419240};
DE AltName: Full=DNA-directed RNA polymerase subunit beta;
GN Name=rpo2 {ECO:0000303|PubMed:19419240};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1] {ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS)
RP OF THE RNA POLYMERASE COMPLEX IN COMPLEX WITH ZINC, FUNCTION, COFACTOR,
RP SUBUNIT, AND NOMENCLATURE.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=19419240; DOI=10.1371/journal.pbio.1000102;
RA Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I.,
RA Sigler P.B., Bell S.D., Abrescia N.G.;
RT "Evolution of complex RNA polymerases: the complete archaeal RNA polymerase
RT structure.";
RL PLoS Biol. 7:e1000102-e1000102(2009).
RN [2] {ECO:0007744|PDB:2Y0S}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH ZINC, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=21265742; DOI=10.1042/bst0390025;
RA Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D., Abrescia N.G.;
RT "Archaeal RNA polymerase: the influence of the protruding stalk in crystal
RT packing and preliminary biophysical analysis of the Rpo13 subunit.";
RL Biochem. Soc. Trans. 39:25-30(2011).
RN [3] {ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH ZINC WITH AND WITHOUT DNA, FUNCTION, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=22848102; DOI=10.1093/nar/gks692;
RA Wojtas M.N., Mogni M., Millet O., Bell S.D., Abrescia N.G.;
RT "Structural and functional analyses of the interaction of archaeal RNA
RT polymerase with DNA.";
RL Nucleic Acids Res. 40:9941-9952(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates (Probable). This subunit is involved in DNA
CC promoter recognition (PubMed:22848102). {ECO:0000269|PubMed:22848102,
CC ECO:0000305|PubMed:19419240, ECO:0000305|PubMed:21265742,
CC ECO:0000305|PubMed:22848102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000305|PubMed:19419240,
CC ECO:0000305|PubMed:21265742, ECO:0000305|PubMed:22848102};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19419240};
CC Note=Binds at least 1 Zn(2+) ion per subunit.
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102};
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:19419240, ECO:0000269|PubMed:21265742,
CC ECO:0000269|PubMed:22848102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22848102}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; FJ515667; ACL36490.1; -; Genomic_DNA.
DR PDB; 2WAQ; X-ray; 3.35 A; B=1-1131.
DR PDB; 2WB1; X-ray; 3.52 A; B/R=1-1131.
DR PDB; 2Y0S; X-ray; 3.80 A; B/R=1-1131.
DR PDB; 4AYB; X-ray; 3.20 A; B=1-1131.
DR PDB; 4V8S; X-ray; 4.32 A; AR/BB=1-1131.
DR PDBsum; 2WAQ; -.
DR PDBsum; 2WB1; -.
DR PDBsum; 2Y0S; -.
DR PDBsum; 4AYB; -.
DR PDBsum; 4V8S; -.
DR SMR; B8YB55; -.
DR BRENDA; 2.7.7.6; 6162.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR019969; RNAP_Rpo2.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1131
FT /note="DNA-directed RNA polymerase subunit Rpo2"
FT /id="PRO_0000453794"
FT BINDING 181
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 184..185
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 209
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 438..442
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 438..440
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 1030..1035
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000305|PubMed:22848102"
FT BINDING 1064
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 1067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 1082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2WAQ, ECO:0007744|PDB:2WB1,
FT ECO:0007744|PDB:2Y0S, ECO:0007744|PDB:4AYB,
FT ECO:0007744|PDB:4V8S"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:4AYB, ECO:0007744|PDB:4V8S"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 311..330
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 349..375
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 465..469
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 536..549
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 578..591
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 607..612
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 647..650
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 666..675
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 685..688
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 693..700
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 709..713
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 722..729
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 741..744
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 745..748
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 749..753
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 755..764
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 789..792
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:2WAQ"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 848..857
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 863..873
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 880..883
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 888..895
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 897..899
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 900..903
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 910..912
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 919..922
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 924..939
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 947..950
FT /evidence="ECO:0007829|PDB:2WAQ"
FT HELIX 954..962
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 976..978
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 986..997
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 1000..1003
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1005..1009
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 1033..1042
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 1045..1051
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 1052..1056
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1058..1063
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1072..1074
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 1075..1078
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1086..1089
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1092..1097
FT /evidence="ECO:0007829|PDB:4AYB"
FT HELIX 1098..1108
FT /evidence="ECO:0007829|PDB:4AYB"
FT TURN 1109..1111
FT /evidence="ECO:0007829|PDB:4AYB"
FT STRAND 1113..1122
FT /evidence="ECO:0007829|PDB:4AYB"
SQ SEQUENCE 1131 AA; 127409 MW; E1761EF2A050BBEB CRC64;
MNELSSNLSI DERWKVIEAY FKSKGLVRQH LDSYNDFVRN KLQEIIDEQG EIPTEIPGLK
VRLGKIRIGK PRVRESDRGE REISPMEARL RNLTYAAPLW LTMIPVENNI EAEPEEVYIG
DLPIMLKSAI DPISQYTLDK LIEIGEDPKD PGGYFIVNGS ERVIVTQEDL APNRVLVDTG
KTGSNITHTA KIISSTAGYR VPVTIERLKD GTFHVSFPAV PGKIPFVILM RALGILTDRD
IVYAVSLDPE IQNELFPSLE QASSIANVDD ALDFIGSRVA IGQKRENRIE KAQQIIDKYF
LPHLGTSADD RRKKAYYLAY AISKVIELYL GRREPDDKDH YANKRLRLAG DLFASLFRVA
FKAFVKDLTY QLEKSKVRGR KLALKALVRP DIVTERIRHA LATGNWVGGR TGVSQLLDRT
NWLSMLSHLR RVISSLARGQ PNFEARDLHG TQWGRMCPFE TPEGPNSGLV KNLALMAQIA
VGINEKIVEK TLYEMGVVPV EEVIRRVTEG GEDQNEYLKW SKVILNGRLV GYYRDGEELA
KKIRERRRKG EISDEVNVGH IVTDFINEVH VNCDSGRVRR PLIIVSNGNP LVTREDIEKL
DSGSITFDDL VRQGKIEYLD AEEEENAYVA LEPSDLTPEH THLEIWSPAI LGITASIIPY
PEHNQSPRNT YQSAMAKQAL GLYAANYQLR TDTRAHLLHY PQRPLVQTRA LDIIGYTNRP
AGNNAILAVI SFTGYNMEDS IIMNRSSVER GMYRSTFFRL YSTEEVKYPG GQEDKIVMPE
PGVRGYKGKE YYRLLEDNGV VSPEVEVKGG DVLIGKVSPP RFLQEFKELS PEQAKRDTSI
VTRHGEMGIV DLVLITETAE GNKLVKVRVR DLRIPSIGDK FASRHGQKGV IGMLIPQVDM
PYTVKGVVPD VILNPHALPS RMTLGQIMEG IAGKYAALSG NIVDATPFYK TPIEQLQNEI
LKYGYLPDAT EVTYDGRTGQ KIKSRIYFGV VYYQKLHHMV ADKIHARARG PVQILTRQPT
EGRAREGGLR FGEMERDCLI GFGTAMLLKD RLLDNSDRTT IYVCDQCGYI GWYDKNKNKY
VCPIHGDKSN LFPVTVSYAF KLLIQELMSM IISPRLILED RVGLSGGKGN E
