RENT1_YEAST
ID RENT1_YEAST Reviewed; 971 AA.
AC P30771; D6VZQ4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=ATP-dependent helicase NAM7;
DE EC=3.6.4.12 {ECO:0000269|PubMed:30218034};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q92900};
DE AltName: Full=Nonsense-mediated mRNA decay protein 1;
DE AltName: Full=Nuclear accommodation of mitochondria 7 protein;
DE AltName: Full=Up-frameshift suppressor 1;
GN Name=NAM7;
GN Synonyms=IFS2, MOF4 {ECO:0000303|PubMed:8896465},
GN UPF1 {ECO:0000303|PubMed:8896465}; OrderedLocusNames=YMR080C;
GN ORFNames=YM9582.05C;
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].
RC STRAIN=R23/50;
RX PubMed=1314899; DOI=10.1016/0022-2836(92)90545-u;
RA Altamura N., Groudinsky O., Dujardin G., Slonimski P.P.;
RT "NAM7 nuclear gene encodes a novel member of a family of helicases with a
RT Zn-ligand motif and is involved in mitochondrial functions in Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 224:575-587(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1569946; DOI=10.1128/mcb.12.5.2165-2177.1992;
RA Leeds P.F., Wood J.M., Lee B.S., Culbertson M.R.;
RT "Gene products that promote mRNA turnover in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:2165-2177(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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.
RX PubMed=7545033; DOI=10.1091/mbc.6.5.611;
RA Atkin A.L., Altamura N., Leeds P., Culbertson M.R.;
RT "The majority of yeast UPF1 co-localizes with polyribosomes in the
RT cytoplasm.";
RL Mol. Biol. Cell 6:611-625(1995).
RN [6]
RP FUNCTION.
RX PubMed=8896465; DOI=10.1002/j.1460-2075.1996.tb00956.x;
RA Cui Y., Dinman J.D., Peltz S.W.;
RT "Mof4-1 is an allele of the UPF1/IFS2 gene which affects both mRNA turnover
RT and -1 ribosomal frameshifting efficiency.";
RL EMBO J. 15:5726-5736(1996).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-484; LYS-485 AND
RP ARG-487.
RX PubMed=30218034; DOI=10.1038/s41467-018-06313-y;
RA Kanaan J., Raj S., Decourty L., Saveanu C., Croquette V., Le Hir H.;
RT "UPF1-like helicase grip on nucleic acids dictates processivity.";
RL Nat. Commun. 9:3752-3752(2018).
CC -!- FUNCTION: RNA-dependent helicase required for nonsense-mediated decay
CC (NMD) of aberrant mRNAs containing premature stop codons and modulates
CC the expression level of normal mRNAs (PubMed:8896465, PubMed:30218034).
CC Also capable of unwinding double-stranded DNA and translocating on
CC single-stranded DNA (PubMed:30218034). {ECO:0000269|PubMed:30218034,
CC ECO:0000269|PubMed:8896465}.
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:0000269|PubMed:30218034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:30218034};
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:0000250|UniProtKB:Q92900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q92900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7545033}.
CC Note=Associates with polysomes. {ECO:0000269|PubMed:7545033}.
CC -!- MISCELLANEOUS: Present with 6090 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; X62394; CAA44266.1; -; Genomic_DNA.
DR EMBL; M76659; AAA35197.1; -; Genomic_DNA.
DR EMBL; Z49259; CAA89226.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09978.1; -; Genomic_DNA.
DR PIR; S23408; S23408.
DR RefSeq; NP_013797.1; NM_001182579.1.
DR PDB; 2XZL; X-ray; 2.40 A; A=54-850.
DR PDBsum; 2XZL; -.
DR AlphaFoldDB; P30771; -.
DR SMR; P30771; -.
DR BioGRID; 35256; 855.
DR ComplexPortal; CPX-1315; Nonsense-mediated decay complex.
DR DIP; DIP-2373N; -.
DR IntAct; P30771; 30.
DR MINT; P30771; -.
DR STRING; 4932.YMR080C; -.
DR iPTMnet; P30771; -.
DR MaxQB; P30771; -.
DR PaxDb; P30771; -.
DR PRIDE; P30771; -.
DR EnsemblFungi; YMR080C_mRNA; YMR080C; YMR080C.
DR GeneID; 855104; -.
DR KEGG; sce:YMR080C; -.
DR SGD; S000004685; NAM7.
DR VEuPathDB; FungiDB:YMR080C; -.
DR eggNOG; KOG1802; Eukaryota.
DR GeneTree; ENSGT00940000157413; -.
DR HOGENOM; CLU_001666_4_1_1; -.
DR InParanoid; P30771; -.
DR OMA; HHDSIGY; -.
DR BioCyc; YEAST:G3O-32782-MON; -.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P30771; -.
DR PRO; PR:P30771; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P30771; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071026; P:cytoplasmic RNA surveillance; IC:ComplexPortal.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IMP:SGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0006449; P:regulation of translational termination; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:SGD.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..971
FT /note="ATP-dependent helicase NAM7"
FT /id="PRO_0000080713"
FT DOMAIN 54..208
FT /note="Upf1 CH-rich"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..94
FT /note="C3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 76..104
FT /note="CC/SHH/C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT REGION 122..152
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 433..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 769
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 484
FT /note="A->H: Decreases binding to substrate."
FT /evidence="ECO:0000269|PubMed:30218034"
FT MUTAGEN 485
FT /note="K->P: Decreases binding to substrate."
FT /evidence="ECO:0000269|PubMed:30218034"
FT MUTAGEN 487
FT /note="R->S: Decreases binding to substrate."
FT /evidence="ECO:0000269|PubMed:30218034"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 149..154
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 235..257
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 436..451
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 499..504
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 510..521
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 526..545
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 548..553
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 579..586
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 590..597
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 609..613
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 642..652
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:2XZL"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 703..718
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 733..746
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 751..755
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 757..761
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 762..765
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 770..776
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 787..790
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 792..799
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 800..810
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 812..815
FT /evidence="ECO:0007829|PDB:2XZL"
FT HELIX 819..831
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 834..838
FT /evidence="ECO:0007829|PDB:2XZL"
FT STRAND 841..844
FT /evidence="ECO:0007829|PDB:2XZL"
SQ SEQUENCE 971 AA; 109430 MW; 9161AFB0BE6747FE CRC64;
MVGSGSHTPY DISNSPSDVN VQPATQLNST LVEDDDVDNQ LFEEAQVTET GFRSPSASDN
SCAYCGIDSA KCVIKCNSCK KWFCNTKNGT SSSHIVNHLV LSHHNVVSLH PDSDLGDTVL
ECYNCGRKNV FLLGFVSAKS EAVVVLLCRI PCAQTKNANW DTDQWQPLIE DRQLLSWVAE
QPTEEEKLKA RLITPSQISK LEAKWRSNKD ATINDIDAPE EQEAIPPLLL RYQDAYEYQR
SYGPLIKLEA DYDKQLKESQ ALEHISVSWS LALNNRHLAS FTLSTFESNE LKVAIGDEMI
LWYSGMQHPD WEGRGYIVRL PNSFQDTFTL ELKPSKTPPP THLTTGFTAE FIWKGTSYDR
MQDALKKFAI DKKSISGYLY YKILGHQVVD ISFDVPLPKE FSIPNFAQLN SSQSNAVSHV
LQRPLSLIQG PPGTGKTVTS ATIVYHLSKI HKDRILVCAP SNVAVDHLAA KLRDLGLKVV
RLTAKSREDV ESSVSNLALH NLVGRGAKGE LKNLLKLKDE VGELSASDTK RFVKLVRKTE
AEILNKADVV CCTCVGAGDK RLDTKFRTVL IDESTQASEP ECLIPIVKGA KQVILVGDHQ
QLGPVILERK AADAGLKQSL FERLISLGHV PIRLEVQYRM NPYLSEFPSN MFYEGSLQNG
VTIEQRTVPN SKFPWPIRGI PMMFWANYGR EEISANGTSF LNRIEAMNCE RIITKLFRDG
VKPEQIGVIT PYEGQRAYIL QYMQMNGSLD KDLYIKVEVA SVDAFQGREK DYIILSCVRA
NEQQAIGFLR DPRRLNVGLT RAKYGLVILG NPRSLARNTL WNHLLIHFRE KGCLVEGTLD
NLQLCTVQLV RPQPRKTERP MNAQFNVESE MGDFPKFQDF DAQSMVSFSG QIGDFGNAFV
DNTELSSYIN NEYWNFENFK SAFSQKQNRN EIDDRNLYQE EASHLNSNFA RELQREEQKH
ELSKDFSNLG I
