ORC1A_ARATH
ID ORC1A_ARATH Reviewed; 809 AA.
AC Q710E8; O23326; Q94G49;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Origin of replication complex subunit 1A {ECO:0000303|PubMed:16179646};
DE Short=AtORC1a {ECO:0000303|PubMed:16179646};
DE AltName: Full=Origin recognition complex subunit 1a {ECO:0000303|Ref.2};
GN Name=ORC1A {ECO:0000303|PubMed:16179646};
GN OrderedLocusNames=At4g14700 {ECO:0000312|Araport:AT4G14700};
GN ORFNames=dl3390w {ECO:0000312|EMBL:CAB10249.1},
GN FCAALL.93 {ECO:0000312|EMBL:CAB78512.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH ORC2; ORC3; ORC4 AND
RP ORC5, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY E2F AND
RP SUCROSE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16179646; DOI=10.1093/nar/gki854;
RA Diaz-Trivino S., Castellano M.M., Sanchez M.P., Ramirez-Parra E.,
RA Desvoyes B., Gutierrez C.;
RT "The genes encoding Arabidopsis ORC subunits are E2F targets and the two
RT ORC1 genes are differently expressed in proliferating and endoreplicating
RT cells.";
RL Nucleic Acids Res. 33:5404-5414(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ramos G.B.A., Cabral L.M., Ferreira P.C.G., Hemerly A.S.;
RT "Isolation of an orc1 homolog from Arabidopsis thaliana.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP SUBUNIT, TISSUE SPECIFICITY, INDUCTION BY SUCROSE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15358564; DOI=10.1016/j.febslet.2004.07.088;
RA Masuda H.P., Ramos G.B.A., de Almeida-Engler J., Cabral L.M.,
RA Coqueiro V.M., Macrini C.M.T., Ferreira P.C.G., Hemerly A.S.;
RT "Genome based identification and analysis of the pre-replicative complex of
RT Arabidopsis thaliana.";
RL FEBS Lett. 574:192-202(2004).
RN [7]
RP REVIEW ON THE CORE DNA REPLICATION MACHINERY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19171893; DOI=10.1073/pnas.0811093106;
RA de la Paz Sanchez M., Gutierrez C.;
RT "Arabidopsis ORC1 is a PHD-containing H3K4me3 effector that regulates
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2065-2070(2009).
RN [9]
RP INTERACTION WITH H3.
RX PubMed=26876097; DOI=10.1016/j.str.2016.01.004;
RA Li S., Yang Z., Du X., Liu R., Wilkinson A.W., Gozani O., Jacobsen S.E.,
RA Patel D.J., Du J.;
RT "Structural basis for the unique multivalent readout of unmodified H3 tail
RT by Arabidopsis ORC1b BAH-PHD cassette.";
RL Structure 24:486-494(2016).
CC -!- FUNCTION: Essential protein (PubMed:19171893). Component of the origin
CC recognition complex (ORC) that binds origins of replication. It has a
CC role in both chromosomal replication and mating type transcriptional
CC silencing. Binds to the ARS consensus sequence (ACS) of origins of
CC replication (By similarity). H3K4me3 effector that regulates positively
CC the transcription of a subset of genes (PubMed:19171893).
CC {ECO:0000250|UniProtKB:P54784, ECO:0000269|PubMed:19171893}.
CC -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC at least ORC1 (ORC1A or ORC1B), ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is
CC regulated in a cell-cycle and development dependent manner. It is
CC sequentially assembled at the exit from anaphase of mitosis and
CC disassembled as cells enter S phase. Interacts directly with ORC2,
CC ORC3, ORC4 and ORC5 (PubMed:16179646, PubMed:15358564). Binds mostly
CC unmodified histone H3, and, with lower efficiency, H3K4me1 H3K4me2 and
CC H3K4me3 (PubMed:26876097). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16179646, ECO:0000269|PubMed:26876097}.
CC -!- INTERACTION:
CC Q710E8; B7U179: ABAP1; NbExp=9; IntAct=EBI-2651718, EBI-541722;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54789}.
CC -!- TISSUE SPECIFICITY: Follow a cell-cycle regulation with a peak at the
CC G1/S-phase (PubMed:16179646). Mostly expressed in siliques, flowers and
CC flower buds, and, to a lower extent, in roots, leaves and stems
CC (PubMed:16179646, PubMed:15358564). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16179646}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in endoreplicating cells,
CC such as cells of the apical hook of dark-grown seedlings.
CC {ECO:0000269|PubMed:16179646}.
CC -!- INDUCTION: Regulated by E2F (PubMed:16179646). Accumulates rapidly
CC after cell cycle reactivation by sucrose addition following cell cycle
CC arrest mediated by sucrose deprivation (PubMed:16179646,
CC PubMed:15358564). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16179646}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000303|PubMed:19171893}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10249.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ421410; CAD13174.1; -; mRNA.
DR EMBL; AF277982; AAK69447.1; -; mRNA.
DR EMBL; Z97336; CAB10249.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83478.1; -; Genomic_DNA.
DR PIR; G71409; G71409.
DR RefSeq; NP_567440.1; NM_117553.2.
DR AlphaFoldDB; Q710E8; -.
DR SMR; Q710E8; -.
DR DIP; DIP-61909N; -.
DR IntAct; Q710E8; 8.
DR MINT; Q710E8; -.
DR STRING; 3702.AT4G14700.1; -.
DR PaxDb; Q710E8; -.
DR PRIDE; Q710E8; -.
DR ProteomicsDB; 248643; -.
DR EnsemblPlants; AT4G14700.1; AT4G14700.1; AT4G14700.
DR GeneID; 827121; -.
DR Gramene; AT4G14700.1; AT4G14700.1; AT4G14700.
DR KEGG; ath:AT4G14700; -.
DR Araport; AT4G14700; -.
DR TAIR; locus:2130090; AT4G14700.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_010923_0_0_1; -.
DR InParanoid; Q710E8; -.
DR OMA; EGDWICH; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; Q710E8; -.
DR PRO; PR:Q710E8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q710E8; baseline and differential.
DR Genevisible; Q710E8; AT.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IBA:GO_Central.
DR GO; GO:0000808; C:origin recognition complex; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:TAIR.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..809
FT /note="Origin of replication complex subunit 1A"
FT /id="PRO_0000431426"
FT DOMAIN 223..341
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 163..213
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..185
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 201..205
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 316..321
FT /note="Histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT REGION 431..799
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SU24"
FT BINDING 466..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 466..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT CONFLICT 5
FT /note="L -> P (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> E (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..73
FT /note="GKESV -> ERESI (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="K -> M (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="L -> V (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="K -> M (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="S -> P (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="V -> A (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="L -> F (in Ref. 2; AAK69447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 91896 MW; 85698C9B8BF0AB42 CRC64;
MASSLSSKAK TFKSPTKTPT KMYRKSYLSP SSTSLTPPQT PETLTPLRRS SRHVSRKINL
GNDPIDLPGK ESVEEINLIR KPRKRTNDIV VAEKSKKKKI DPEVSFSPVS PIRSETKKTK
KKKRVYYNKV EFDETEFEIG DDVYVKRTED ANPDEEEEED PEIEDCQICF KSHTNTIMIE
CDDCLGGFHL NCLKPPLKEV PEGDWICQFC EVKKSGQTLV VVPKPPEGKK LARTMKEKLL
SSDLWAARIE KLWKEVDDGV YWIRARWYMI PEETVLGRQR HNLKRELYLT NDFADIEMEC
VLRHCFVKCP KEFSKASNDG DDVFLCEYEY DVHWGSFKRV AELADGDEDS DQEWNGRKEE
EIDYSDEEIE FDDEESVRGV SKSKRGGANS RKGRFFGLEK VGMKRIPEHV RCHKQSELEK
AKATLLLATR PKSLPCRSKE MEEITAFIKG SISDDQCLGR CMYIHGVPGT GKTISVLSVM
KNLKAEVEAG SVSPYCFVEI NGLKLASPEN IYSVIYEGLS GHRVGWKKAL QSLNERFAEG
KKIGKENEKP CILLIDELDV LVTRNQSVLY NILDWPTKPN SKLVVLGIAN TMDLPEKLLP
RISSRMGIQR LCFGPYNHRQ LQEIISTRLE GINAFEKTAI EFASRKVAAI SGDARRALEI
CRRAAEVADY RLKKSNISAK SQLVIMADVE VAIQEMFQAP HIQVMKSVSK LSRIFLTAMV
HELYKTGMAE TSFDRVATTV SSICLTNGEA FPGWDILLKI GCDLGECRIV LCEPGEKHRL
QKLQLNFPSD DVAFALKDNK DLPWLANYL
