REH2_TRYB2
ID REH2_TRYB2 Reviewed; 2167 AA.
AC Q581T1; D6XF86;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=RNA editing associated helicase 2 {ECO:0000303|PubMed:19850921};
DE EC=3.6.4.13 {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:31034523, ECO:0000305|PubMed:26769962};
DE AltName: Full=ATP-dependent RNA helicase REH2 {ECO:0000305};
DE Flags: Precursor;
GN Name=REH2 {ECO:0000303|PubMed:19850921};
GN ORFNames=Tb927.4.1500 {ECO:0000312|EMBL:AAX79889.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|EMBL:AAX79889.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAX79889.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAZ10741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ10741.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [3] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH THE RECC COMPLEX,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, MOTIF, IDENTIFICATION BY
RP MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 1026-LYS--LEU-1092 AND 1366-GLY-LYS-1367.
RC STRAIN=427 {ECO:0000269|PubMed:19850921};
RX PubMed=19850921; DOI=10.1074/jbc.m109.051862;
RA Hernandez A., Madina B.R., Ro K., Wohlschlegel J.A., Willard B.,
RA Kinter M.T., Cruz-Reyes J.;
RT "REH2 RNA helicase in kinetoplastid mitochondria: ribonucleoprotein
RT complexes and essential motifs for unwinding and guide RNA (gRNA)
RT binding.";
RL J. Biol. Chem. 285:1220-1228(2010).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH THE GRBC COMPLEX, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-1078; ALA-1086 AND 1366-GLY-LYS-1367.
RC STRAIN=427 {ECO:0000269|PubMed:25928631};
RX PubMed=25928631; DOI=10.1371/journal.pone.0123441;
RA Madina B.R., Kumar V., Mooers B.H., Cruz-Reyes J.;
RT "Native Variants of the MRB1 Complex Exhibit Specialized Functions in
RT Kinetoplastid RNA Editing.";
RL PLoS ONE 10:e0123441-e0123441(2015).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE REH2C COMPLEX,
RP INTERACTION WITH THE GRBC COMPLEX; RECC COMPLEX; REMC COMPLEX AND H2F1,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000269|PubMed:26769962};
RX PubMed=26769962; DOI=10.1074/jbc.m115.708164;
RA Kumar V., Madina B.R., Gulati S., Vashisht A.A., Kanyumbu C., Pieters B.,
RA Shakir A., Wohlschlegel J.A., Read L.K., Mooers B.H.M., Cruz-Reyes J.;
RT "REH2C Helicase and GRBC Subcomplexes May Base Pair through mRNA and Small
RT Guide RNA in Kinetoplastid Editosomes.";
RL J. Biol. Chem. 291:5753-5764(2016).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE REH2C COMPLEX,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 34-GLN--LEU-1093; 34-GLN--PRO-1023; LYS-1078; ALA-1086; 1908-THR--SER-2167;
RP ARG-1979; HIS-1998; ARG-1999; ARG-2023 AND 2045-MET--SER-2167.
RC STRAIN=427 {ECO:0000269|PubMed:31034523};
RX PubMed=31034523; DOI=10.1371/journal.pone.0211525;
RA Kumar V., Doharey P.K., Gulati S., Meehan J., Martinez M.G., Hughes K.,
RA Mooers B.H.M., Cruz-Reyes J.;
RT "Protein features for assembly of the RNA editing helicase 2 subcomplex
RT (REH2C) in Trypanosome holo-editosomes.";
RL PLoS ONE 14:e0211525-e0211525(2019).
CC -!- FUNCTION: ATP-dependent RNA helicase that unwinds RNA in a 3' to 5'
CC direction and that plays an important role in mitochondrial mRNA
CC editing, a process involving the addition and deletion of uridine (U)
CC nucleotides in the pre-mRNA (PubMed:19850921, PubMed:26769962,
CC PubMed:31034523). As part of the RET2-containing gRNA-binding (RET2-
CC GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids
CC and the recruitment of the RNA editing core (RECC) complex
CC (PubMed:25928631, PubMed:26769962). Regulates several steps of mRNA
CC editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC)
CC complex including loading of unedited mRNA, editing in the first
CC sequence block and subsequent editing progression across multiple
CC sequence blocks (PubMed:25928631). Also, regulates the RNA substrate
CC content of the MRBC3010-GRBC complex as well as the association of this
CC complex with mitoribosomes (PubMed:25928631).
CC {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:25928631,
CC ECO:0000269|PubMed:26769962, ECO:0000269|PubMed:31034523}.
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=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:31034523,
CC ECO:0000305|PubMed:26769962};
CC -!- SUBUNIT: Component of the REH2-associated complex (REH2C) composed of
CC helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various
CC editing stages; the formation of the complex is RNA-independent
CC (PubMed:26769962, PubMed:31034523). Within the complex, interacts with
CC H2F1; the interaction is direct (PubMed:26769962, PubMed:31034523).
CC Interacts transiently, in a RNA-dependent manner, with various editing
CC complexes including the RNA editing core (RECC) complex, the gRNA-
CC binding (GRBC) complex (also known as the MRB1 complex) and the RNA
CC editing mediator (REMC) complex (PubMed:19850921, PubMed:25928631,
CC PubMed:26769962, PubMed:31034523). Interacts with GAP1/GRBC2 via RNA
CC forming a variant of the GRBC complex known as REH2-GRBC complex
CC (PubMed:19850921, PubMed:25928631, PubMed:26769962, PubMed:31034523).
CC Interacts with mitochondrial ribosomes (PubMed:19850921).
CC {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:25928631,
CC ECO:0000269|PubMed:26769962, ECO:0000269|PubMed:31034523}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19850921,
CC ECO:0000269|PubMed:25928631, ECO:0000269|PubMed:26769962,
CC ECO:0000269|PubMed:31034523}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the procyclic stage (at protein
CC level). {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:25928631,
CC ECO:0000269|PubMed:26769962, ECO:0000269|PubMed:31034523}.
CC -!- DOMAIN: The DRBM domain is required for binding to guide RNAs (gRNA)
CC and mRNAs which facilitates the association with the GRBC complex.
CC {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:25928631}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the procyclic stage
CC causes a loss of RNA unwinding activity (PubMed:26769962). Reduces
CC association of H2F1 and abolishes H2F2 association with components of
CC various editing complexes (PubMed:26769962). RNAi-mediated knockdown at
CC the procyclic stage inhibits editing at early 3' sites on pre-mRNA
CC substrates without affecting the interactions between MRB3010/GRBC6,
CC GAP1/GRBC2, RGG2, REL1 and gRNA (PubMed:25928631). Decreases the ratio
CC of unedited mRNA substrates in the MRB3010/GRBC6-MRB complex and the
CC association of never-edited mRNA and 9SrRNA with the MRB3010-MRB
CC complex (PubMed:25928631). Also, causes a decrease in the steady-state
CC levels of guide RNA (gRNA) (PubMed:19850921).
CC {ECO:0000269|PubMed:19850921, ECO:0000269|PubMed:25928631,
CC ECO:0000269|PubMed:26769962}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AC091702; AAX79889.1; -; Genomic_DNA.
DR EMBL; CP000067; AAZ10741.1; -; Genomic_DNA.
DR RefSeq; XP_844300.1; XM_839207.1.
DR AlphaFoldDB; Q581T1; -.
DR SMR; Q581T1; -.
DR STRING; 5691.AAZ10741; -.
DR PaxDb; Q581T1; -.
DR GeneID; 3656679; -.
DR KEGG; tbr:Tb927.4.1500; -.
DR VEuPathDB; TriTrypDB:Tb927.4.1500; -.
DR eggNOG; KOG0920; Eukaryota.
DR InParanoid; Q581T1; -.
DR OMA; SRANCVQ; -.
DR Proteomes; UP000008524; Chromosome 4.
DR GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR GO; GO:0031019; C:mitochondrial mRNA editing complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR GO; GO:0003723; F:RNA binding; IDA:GeneDB.
DR GO; GO:0016554; P:cytidine to uridine editing; IDA:GeneDB.
DR GO; GO:0000963; P:mitochondrial RNA processing; IDA:UniProtKB.
DR GO; GO:0016556; P:mRNA modification; IMP:GeneDB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IDA:GeneDB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; mRNA processing;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..2167
FT /note="RNA editing associated helicase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455617"
FT DOMAIN 1024..1095
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 1348..1513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1585..1762
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 503..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2132..2167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1366..1367
FT /note="Important for binding to gRNA"
FT /evidence="ECO:0000269|PubMed:19850921"
FT MOTIF 1460..1463
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 524..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1361..1368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 34..1093
FT /note="Missing: Severe reduction in the interaction with
FT H2F1 and GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 34..1023
FT /note="Missing: Severe reduction in the interaction with
FT H2F1 and GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 1026..1092
FT /note="KTVLQRYCNVANVNYPTFWKSRTVGPISCRVCLTTIEVPGHEYLRASGVAWN
FT KEASQRQAAMHALAL->TR: Loss of RNA helicase activity. Loss of
FT binding to gRNA. Impaired association with several mRNA
FT editing complexes."
FT /evidence="ECO:0000269|PubMed:19850921"
FT MUTAGEN 1078
FT /note="K->A: Loss of interaction with gRNA, unedited mRNAs,
FT edited mRNAs at block 1 or at 5' distal blocks, and
FT GAP1/GRBC2 but not with H2F1; when associated with A-1086."
FT /evidence="ECO:0000269|PubMed:25928631,
FT ECO:0000269|PubMed:31034523"
FT MUTAGEN 1086
FT /note="A->D: Loss of interaction with gRNA, unedited mRNAs,
FT edited mRNAs at block 1 or at 5' distal blocks, and
FT GAP1/GRBC2 but not with H2F1; when associated with A-1078."
FT /evidence="ECO:0000269|PubMed:25928631,
FT ECO:0000269|PubMed:31034523"
FT MUTAGEN 1366..1367
FT /note="GK->AQ: Loss of RNA helicase activity. Loss of
FT interaction with gRNA, unedited mRNAs and edited mRNAs at
FT block 1 or at 5' distal blocks. Loss of interaction with
FT GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:19850921,
FT ECO:0000269|PubMed:25928631"
FT MUTAGEN 1908..2167
FT /note="Missing: Severe reduction in the interaction with
FT H2F1 and GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 1979
FT /note="R->A: Does not affect the interaction with H2F1 and
FT GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 1998
FT /note="H->E: Moderate reduction in the interaction with
FT GAP1/GRBC2. Interaction with H2F1 is normal. Severe
FT reduction in the interaction with H2F1 and GAP1/GRBC2; when
FT associated with E-1999."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 1999
FT /note="R->E: Reduction in the interaction with H2F1 and
FT GAP1/GRBC2. Severe reduction in the interaction with H2F1
FT and GAP1/GRBC2; when associated with E-1998."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 2023
FT /note="R->A: Moderate reduction in the interaction with
FT GAP1/GRBC2. Interaction with H2F1 is normal."
FT /evidence="ECO:0000269|PubMed:31034523"
FT MUTAGEN 2045..2167
FT /note="Missing: Severe reduction in the interaction with
FT H2F1 and GAP1/GRBC2."
FT /evidence="ECO:0000269|PubMed:31034523"
SQ SEQUENCE 2167 AA; 241824 MW; 9E4F9535817DE130 CRC64;
MRAIRLTVAC RYLGPFRSVT LSPVVLPVRL FQTQEITPGE VSLVEATDES DRAFGETRKE
DFSFDGSSEF PECFKDTKHV DTFSRARVVS FIKRFSQGAV TSSSEVFEGR EIVNDNGTPL
YHSRVRLPFR SHTGELWAHG VACNSKDAEL LAAMHAEHII DEFGYHIYTL PSMQRKHAEA
ARKAGRWAPL PDELERTQSP VRVPLPLRRI VDRDETEGGK WLLIDMRPNH YISPSHTLLS
PCLFDTTAVH RIKSFLDEHK LSFAQLCTSV EEPGEGGGQS WYVATVSLPP ELSTFSEIKA
QGKALNREAA VTLACMHAEL VLDAHSICLY PSDSTKQKQH ALAAWSYGRP APLPGEDQKN
PSHVVCPLPL KQLAVRREDR ISCISYEEDI IRRHRALTDQ TCEFIETPTL DSSAVEQLKQ
FLQRENVPRT DPFLVEEVNG YYKATVVLPL PDLYGIRGGV GIAMNATDAR VLAAMHAIDV
LNILGFHLMD GSTARAEWIA ARRARGESVP ADTRDPNVLS PSGRRRVATG NSSTQTPSSS
TNARSVAAAP DVGTSDPTAP QNTKRRVAKR ARVADAQPTE EKDAANSDSD EATSYLKMRE
TVSKELWNLE PDSPDGYIMV SPTDPETRTQ FEQALYSPRQ VDLGSKSRIK NYLASVGRRI
EEVFFVQRIE AEDNGGQAIC RCAVNLPVPR RFGDRIALGE AVDPKDAENL AAMHAELILD
TLGIPIYTDS ALQRLHVRLC AKCGRNAPVE YSESVAAATA SPPPLRREVV GSIHWENKSK
RRRAAISVQK GGGPANSQET TSALREDEEP LIAPKERREY TFVPEKDLDL VSRARVHYYL
RRNGIAKLEP EYRMELRGLG NVLHIAELTL PLPDVYGKRV AHGSALTKRD AEILCWMHAE
QILDAVGLCL FDNLPMLQRR HVECVKRLGR WAPLVSENAT KPPHTPTPLP LTLGTTQEKP
QYPTPPTNVR QDWEQYAQEC QRYIEINVMR EHNIFYEMGK TPRTGDETYD AALAEVESMP
IDPDAKTVLQ RYCNVANVNY PTFWKSRTVG PISCRVCLTT IEVPGHEYLR ASGVAWNKEA
SQRQAAMHAL ALLRRVEPDF AEFEKQIKAE VVDKVNLVDP AAVLDEEAPV LRRTARVSKK
SLGNWDPVSK DFSHEGKVRI IELFTVCFGL QPPLVRHLNR RSGSFVQHFT VVEVTDEDGK
TWVGTGRDAG PRFNEPAAFD DLFSKLSRGV QGFQALMDLI RAHPHLDPEH IANVSLTDSQ
KERILKAVDG LPMVEEEDVA HPEQWADADS DRGIGIMALI AMDASQRAQE SQELEAKLQA
KLTNEEYQTR YASQRQRLRI YEKRDEILRA ISSNQIVIIC GTTGCGKTTQ VPQYILDDMT
EKGMGGDCSI VITQPRRLSA VSIARRVAAE RLESIGETCG YSIRLDAKPG RNINFCTSGV
LLRLLHSAPL LNGINYLIID EIHERDINSD FLLILLRQLL HRRKDLHVIL MSATLQADQF
GKYFGNAPII NVEGYVHAVE EMYLEDLVPI ATERNVMTPL LKEAAAALER NGAADGFCPT
VVPPTAKYGF LEATADIDYM TIQIAIDHAV RSLDLTDSSI LVFLPGWDEI NRAKEILERN
AKFHIICLHS SVGAEEQMRC FLPAPEGKIK LILSTNIAES GVTIDDVAAV IDVGRGKEKS
YVMRKGTTSV GRNEMGSMSQ LVTVYASRAN CVQRRGRVGR TRPGMCIRLY SKKHFQSLHD
FQTPEMLRTH LDSLCLQILA LDLGDPADFL QQALEPPSSD HIEAAMKRLH ELGATTSTRQ
LTPLGLRLSR LPVAPKVGKM VIMGAILRCL DSALTIAGVS DTDVFISTRE HREAVRLHKE
DLSYGTQSDV IASVNAFNFW VTSHYAKTPA EVVYDLQERM LSVPQLLTVS KYKQQFFEIV
AGSGFIHMKQ NYKDAKNKDR ADIFVDQSEY SADSLNVGLV KCVVASGLFP NVVMNRGKRL
MRNKLANRLD PSSASVVHRT SQENIGQPYF VYDELVKSSE SERLLVRDLT NVSLWTILLM
GTSSMPVTYR DDLNLAVVDE WIMFRATFGT LELIRKFKRA LNVCLGRKFM NPNDEENNAK
LEELRCIIKE LVCTPFKPND LAEKPWEEKG VIIEPCTEPK GGSSEAEKTH VNSSHTPTTS
AEAGGDS
