QRI7_YEAST
ID QRI7_YEAST Reviewed; 407 AA.
AC P43122; D6VRP6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:23620299};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein QRI7 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein QRI7 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=QRI7; OrderedLocusNames=YDL104C; ORFNames=D2366;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7725801; DOI=10.1002/yea.320101215;
RA Simon M., Benit P., Vassal A., Dubois C., Faye G.;
RT "Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces
RT cerevisiae.";
RL Yeast 10:1653-1656(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896274;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT genes, and six new open reading frames.";
RL Yeast 12:1077-1084(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [8]
RP FUNCTION IN MITOCHONDRIAL GENOME MAINTENANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=19578062; DOI=10.1093/nar/gkp557;
RA Oberto J., Breuil N., Hecker A., Farina F., Brochier-Armanet C.,
RA Culetto E., Forterre P.;
RT "Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein,
RT is essential for mitochondrial genome maintenance.";
RL Nucleic Acids Res. 37:5343-5352(2009).
RN [9]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21183954; DOI=10.1038/emboj.2010.343;
RA Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W.,
RA Sternglanz R.;
RT "The highly conserved KEOPS/EKC complex is essential for a universal tRNA
RT modification, t6A.";
RL EMBO J. 30:873-881(2011).
RN [10]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21285948; DOI=10.1038/emboj.2010.363;
RA El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P.,
RA Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.;
RT "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA
RT modification.";
RL EMBO J. 30:882-893(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 30-407 IN COMPLEX WITH ZINC,
RP CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-39; ASP-43; ASP-44; ILE-77; ARG-104; LYS-130; VAL-134; HIS-145;
RP HIS-149; SER-172; ARG-207; SER-258 AND ASP-361.
RX PubMed=23620299; DOI=10.1093/nar/gkt322;
RA Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I.,
RA Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C.,
RA Caudy A.A., Durocher D., Sicheri F.;
RT "Reconstitution and characterization of eukaryotic N6-
RT threonylcarbamoylation of tRNA using a minimal enzyme system.";
RL Nucleic Acids Res. 41:6332-6346(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 30-407 IN COMPLEX WITH AMP AND
RP ZINC, AND SUBUNIT.
RX PubMed=25084372; DOI=10.1107/s2053230x14014046;
RA Tominaga T., Kobayashi K., Ishii R., Ishitani R., Nureki O.;
RT "Structure of Saccharomyces cerevisiae mitochondrial Qri7 in complex with
RT AMP.";
RL Acta Crystallogr. F 70:1009-1014(2014).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC codons beginning with adenine. Probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC group of A37. Involved in mitochondrial genome maintenance.
CC {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:19578062,
CC ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:21285948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:23620299};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:23620299, ECO:0000269|PubMed:25084372};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179, ECO:0000269|PubMed:23620299,
CC ECO:0000269|PubMed:25084372};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:23620299, ECO:0000269|PubMed:25084372}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:23620299}.
CC -!- DISRUPTION PHENOTYPE: Loss of QRI7 leads to the formation of
CC mitochondria with abnormal morphology and no DNA.
CC {ECO:0000269|PubMed:19578062}.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79380; CAA55926.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64909.1; -; Genomic_DNA.
DR EMBL; Z74152; CAA98671.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11756.1; -; Genomic_DNA.
DR PIR; S50740; S50740.
DR RefSeq; NP_010179.1; NM_001180163.1.
DR PDB; 3WUH; X-ray; 2.94 A; A/B=30-407.
DR PDB; 4K25; X-ray; 2.88 A; A=30-407.
DR PDBsum; 3WUH; -.
DR PDBsum; 4K25; -.
DR AlphaFoldDB; P43122; -.
DR SMR; P43122; -.
DR BioGRID; 31958; 180.
DR DIP; DIP-5028N; -.
DR IntAct; P43122; 1.
DR STRING; 4932.YDL104C; -.
DR MaxQB; P43122; -.
DR PaxDb; P43122; -.
DR PRIDE; P43122; -.
DR EnsemblFungi; YDL104C_mRNA; YDL104C; YDL104C.
DR GeneID; 851454; -.
DR KEGG; sce:YDL104C; -.
DR SGD; S000002262; QRI7.
DR VEuPathDB; FungiDB:YDL104C; -.
DR eggNOG; KOG2707; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_4_1_1; -.
DR OMA; HLEGHIY; -.
DR BioCyc; YEAST:YDL104C-MON; -.
DR BRENDA; 2.3.1.234; 984.
DR PRO; PR:P43122; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P43122; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IDA:SGD.
DR GO; GO:0072670; P:mitochondrial tRNA threonylcarbamoyladenosine modification; IMP:SGD.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:SGD.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Metal-binding; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 31..407
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT /id="PRO_0000096988"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:23620299"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:23620299"
FT BINDING 170..174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 328..329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:25084372"
FT BINDING 361
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179,
FT ECO:0000269|PubMed:23620299"
FT MUTAGEN 39
FT /note="E->A: Severely impairs t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 43
FT /note="D->A: Severely impairs t(6)A37 formation. No effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 44
FT /note="D->A: Severely impairs t(6)A37 formation. No effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 77
FT /note="I->E: Severely impairs t(6)A37 formation. No effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 104
FT /note="R->A: Reduces enzyme activity by 35%. Partially
FT impairs dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 130
FT /note="K->A: Severely impairs t(6)A37 formation. Partially
FT impairs dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 134
FT /note="V->R: Severely impairs t(6)A37 formation. Prevents
FT dimerization."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 145
FT /note="H->A: Severely impairs t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 149
FT /note="H->A: Severely impairs t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 172
FT /note="S->K: Severely impairs t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 207
FT /note="R->A: Severely impairs t(6)A37 formation. No effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 258
FT /note="S->A: Severely impairs t(6)A37 formation. No effect
FT on dimer formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT MUTAGEN 361
FT /note="D->A: Severely impairs t(6)A37 formation."
FT /evidence="ECO:0000269|PubMed:23620299"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 82..99
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4K25"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3WUH"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:4K25"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 281..309
FT /evidence="ECO:0007829|PDB:4K25"
FT TURN 311..316
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:4K25"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3WUH"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4K25"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4K25"
FT TURN 394..398
FT /evidence="ECO:0007829|PDB:4K25"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4K25"
SQ SEQUENCE 407 AA; 45543 MW; 328A21F239D6DB25 CRC64;
MISIKGTGRF LLDNYRIWQR RAFNRPIQLR KGYKVLAIET SCDDTCVSVL DRFSKSAAPN
VLANLKDTLD SIDEGGIIPT KAHIHHQARI GPLTERALIE SNAREGIDLI CVTRGPGMPG
SLSGGLDFAK GLAVAWNKPL IGVHHMLGHL LIPRMGTNGK VPQFPFVSLL VSGGHTTFVL
SRAIDDHEIL CDTIDIAVGD SLDKCGRELG FKGTMIAREM EKFINQDIND QDFALKLEMP
SPLKNSASKR NMLSFSFSAF ITALRTNLTK LGKTEIQELP EREIRSIAYQ VQESVFDHII
NKLKHVLKSQ PEKFKNVREF VCSGGVSSNQ RLRTKLETEL GTLNSTSFFN FYYPPMDLCS
DNSIMIGWAG IEIWESLRLV SDLDICPIRQ WPLNDLLSVD GWRTDQL
