RGYR_ARCFU
ID RGYR_ARCFU Reviewed; 1054 AA.
AC O29238;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Reverse gyrase {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Topoisomerase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01125};
GN Name=rgy {ECO:0000255|HAMAP-Rule:MF_01125}; OrderedLocusNames=AF_1024;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP N-TERMINAL DOMAIN FUNCTIONAL CHARACTERIZATION, AND MUTAGENESIS OF TYR-809.
RX PubMed=12048189; DOI=10.1074/jbc.m202853200;
RA Rodriguez A.C.;
RT "Studies of a positive supercoiling machine. Nucleotide hydrolysis and a
RT multifunctional 'latch' in the mechanism of reverse gyrase.";
RL J. Biol. Chem. 277:29865-29873(2002).
RN [3]
RP N-TERMINAL DOMAIN FUNCTIONAL CHARACTERIZATION.
RX PubMed=12755601; DOI=10.1021/bi034188l;
RA Rodriguez A.C.;
RT "Investigating the role of the latch in the positive supercoiling mechanism
RT of reverse gyrase.";
RL Biochemistry 42:5993-6004(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 38-1054 AND IN COMPLEX WITH
RP ADENYLYLIMIDODIPHOSPHATE (ADPNP).
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=11823434; DOI=10.1093/emboj/21.3.418;
RA Rodriguez A.C., Stock D.;
RT "Crystal structure of reverse gyrase: insights into the positive
RT supercoiling of DNA.";
RL EMBO J. 21:418-426(2002).
CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive
CC supercoils in an ATP-dependent process. It cleaves transiently a single
CC DNA strand and remains covalently bound to the 5' DNA end through a
CC tyrosine residue. May be involved in rewinding the DNA strands in the
CC regions of the chromosome that have opened up to allow transcription or
CC replication.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01125,
CC ECO:0000269|PubMed:11823434}.
CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling activities
CC require the cooperation of both domains. The cooperative action between
CC the helicase-like and the topoisomerase domains is specific. The
CC helicase-like domain probably does not directly unwind DNA but acts
CC more likely by driving ATP-dependent conformational changes within the
CC whole enzyme, functioning more like a protein motor. The 'latch' region
CC of the N-terminal domain plays a regulatory role in the enzyme,
CC repressing topoisomerase activity in the absence of ATP and therefore
CC preventing the enzyme from acting as an ATP-independent relaxing
CC enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase
CC domain with the supercoiling activity of the topoisomerase domain.
CC -!- MISCELLANEOUS: This enzyme is the only unique feature of
CC hyperthermophilic bacteria/archaea discovered so far. It appears to be
CC essential for adaptation to life at high temperatures.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase
CC family. DDVD subfamily. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic type
CC I/III topoisomerase family. {ECO:0000255|HAMAP-Rule:MF_01125}.
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DR EMBL; AE000782; AAB90219.1; -; Genomic_DNA.
DR PIR; H69377; H69377.
DR RefSeq; WP_010878524.1; NC_000917.1.
DR PDB; 1GKU; X-ray; 2.70 A; B=33-1054.
DR PDB; 1GL9; X-ray; 3.20 A; B/C=1-1054.
DR PDBsum; 1GKU; -.
DR PDBsum; 1GL9; -.
DR AlphaFoldDB; O29238; -.
DR SMR; O29238; -.
DR STRING; 224325.AF_1024; -.
DR PRIDE; O29238; -.
DR EnsemblBacteria; AAB90219; AAB90219; AF_1024.
DR GeneID; 1484247; -.
DR KEGG; afu:AF_1024; -.
DR eggNOG; arCOG01526; Archaea.
DR HOGENOM; CLU_002886_0_0_2; -.
DR OMA; GVATYYG; -.
DR OrthoDB; 1837at2157; -.
DR PhylomeDB; O29238; -.
DR BRENDA; 5.6.2.2; 414.
DR EvolutionaryTrace; O29238; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03361; TOPRIM_TopoIA_RevGyr; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01125; Reverse_gyrase; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005736; Reverse_gyrase.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034142; TOPRIM_RevGyr.
DR PANTHER; PTHR43505; PTHR43505; 2.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF01131; Topoisom_bac; 2.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01054; rgy; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1..1054
FT /note="Reverse gyrase"
FT /id="PRO_0000158086"
FT DOMAIN 65..245
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 506..662
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 10..27
FT /note="C4-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 584..601
FT /note="C4-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT REGION 512..1054
FT /note="Topoisomerase I"
FT MOTIF 182..185
FT /note="DEAD box"
FT ACT_SITE 809
FT /note="For DNA cleavage activity"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 633
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT MUTAGEN 809
FT /note="Y->F: Loss of topoisomerase activity."
FT /evidence="ECO:0000269|PubMed:12048189"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1GL9"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1GL9"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1GL9"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1GL9"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1GL9"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:1GL9"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1GL9"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1GL9"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 393..404
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 481..496
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 624..628
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 634..647
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 663..670
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 678..704
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 717..728
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 733..740
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 741..744
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 752..768
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 791..803
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 819..829
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:1GL9"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 855..864
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 874..889
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 895..906
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 909..913
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 916..921
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 922..926
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 939..945
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 948..953
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 958..968
FT /evidence="ECO:0007829|PDB:1GKU"
FT TURN 973..975
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 976..985
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 988..992
FT /evidence="ECO:0007829|PDB:1GKU"
FT STRAND 995..998
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 1000..1011
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 1015..1017
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 1019..1034
FT /evidence="ECO:0007829|PDB:1GKU"
FT HELIX 1039..1051
FT /evidence="ECO:0007829|PDB:1GKU"
SQ SEQUENCE 1054 AA; 121315 MW; 551F19ADD62D7175 CRC64;
MIPVVYSNLC PVCGGDLESK EIEKHVCFRK KRSLCLFPED FLLKEFVEFF RKCVGEPRAI
QKMWAKRILR KESFAATAPT GVGKTSFGLA MSLFLALKGK RCYVIFPTSL LVIQAAETIR
KYAEKAGVGT ENLIGYYHGR IPKREKENFM QNLRNFKIVI TTTQFLSKHY RELGHFDFIF
VDDVDAILKA SKNVDKLLHL LGFHYDLKTK SWVGEARGCL MVSTATAKKG KKAELFRQLL
NFDIGSSRIT VRNVEDVAVN DESISTLSSI LEKLGTGGII YARTGEEAEE IYESLKNKFR
IGIVTATKKG DYEKFVEGEI DHLIGTAHYY GTLVRGLDLP ERIRFAVFVG CPSFRVTIED
IDSLSPQMVK LLAYLYRNVD EIERLLPAVE RHIDEVREIL KKVMGKERPQ AKDVVVREGE
VIFPDLRTYI QGSGRTSRLF AGGLTKGASF LLEDDSELLS AFIERAKLYD IEFKSIDEVD
FEKLSRELDE SRDRYRRRQE FDLIKPALFI VESPTKARQI SRFFGKPSVK VLDGAVVYEI
PMQKYVLMVT ASIGHVVDLI TNRGFHGVLV NGRFVPVYAS IKRCRDCGYQ FTEDRESCPK
CGSENVDNSR SRIEALRKLA HDAEFVIVGT DPDTEGEKIA WDLKNLLSGC GAVKRAEFHE
VTRRAILEAL ESLRDVDENL VKAQVVRRIE DRWIGFVLSQ KLWERFNNRN LSAGRAQTPV
LGWIIDRFQE SRERRKIAIV RDFDLVLEHD EEEFDLTIKL VEEREELRTP LPPYTTETML
SDANRILKFS VKQTMQIAQE LFENGLITYH RTDSTRVSDV GQRIAKEYLG DDFVGREWGE
SGAHECIRPT RPLTRDDVQR LIQEGVLVVE GLRWEHFALY DLIFRRFMAS QCRPFKVVVK
KYSIEFDGKT AEEERIVRAE GRAYELYRAV WVKNELPTGT FRVKAEVKSV PKVLPFTQSE
IIQMMKERGI GRPSTYATIV DRLFMRNYVV EKYGRMIPTK LGIDVFRFLV RRYAKFVSED
RTRDLESRMD AIERGELDYL KALEDLYAEI KSID
