MTR4_YEAST
ID MTR4_YEAST Reviewed; 1073 AA.
AC P47047; D6VWD3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=ATP-dependent RNA helicase DOB1;
DE EC=3.6.4.13;
DE AltName: Full=mRNA transport regulator MTR4;
GN Name=MTR4; Synonyms=DOB1; OrderedLocusNames=YJL050W; ORFNames=J1158;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
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 [3]
RP CHARACTERIZATION.
RX PubMed=8756671; DOI=10.1128/mcb.16.9.5139;
RA Liang S., Hitomi M., Hu Y.-H., Liu Y., Tartakoff A.M.;
RT "A DEAD-box-family protein is required for nucleocytoplasmic transport of
RT yeast mRNA.";
RL Mol. Cell. Biol. 16:5139-5146(1996).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9463390; DOI=10.1093/emboj/17.4.1128;
RA de la Cruz J., Kressler D., Tollervey D., Linder P.;
RT "Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3'
RT end formation of 5.8S rRNA in Saccharomyces cerevisiae.";
RL EMBO J. 17:1128-1140(1998).
RN [5]
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 [6]
RP IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
RA Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
RA Langen H., Keith G., Keller W.;
RT "A new yeast poly(A) polymerase complex involved in RNA quality control.";
RL PLoS Biol. 3:986-997(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84 AND SER-843, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, 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).
CC -!- FUNCTION: ATP-dependent RNA helicase required for the 3'-end formation
CC of 5.8S RNA. Cofactor for the exosome complex that unwinds secondary
CC structure in pre-rRNA. Required for nucleocytoplasmic transport of
CC mRNA. May serve as a chaperone which translocates or normalizes the
CC structure of mRNAs in preparation for export. Component of the TRAMP
CC complex which has a poly(A) RNA polymerase activity and is involved in
CC a post-transcriptional quality control mechanism limiting inappropriate
CC expression of genetic information. Polyadenylation is required for the
CC degradative activity of the exosome on several of its nuclear RNA
CC substrates. {ECO:0000269|PubMed:15828860}.
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 -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
CC {ECO:0000269|PubMed:15828860}.
CC -!- INTERACTION:
CC P47047; Q12476: AIR2; NbExp=7; IntAct=EBI-11592, EBI-31475;
CC P47047; P38074: HMT1; NbExp=2; IntAct=EBI-11592, EBI-8394;
CC P47047; P53632: PAP2; NbExp=11; IntAct=EBI-11592, EBI-19517;
CC P47047; P48561: TRF5; NbExp=6; IntAct=EBI-11592, EBI-19525;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 12500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49325; CAA89341.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08749.1; -; Genomic_DNA.
DR PIR; S56822; S56822.
DR RefSeq; NP_012485.1; NM_001181483.1.
DR PDB; 2XGJ; X-ray; 2.90 A; A/B=81-1073.
DR PDB; 4QU4; X-ray; 3.39 A; A=1-1073.
DR PDB; 4U4C; X-ray; 2.40 A; A=81-1073.
DR PDB; 4WFD; X-ray; 2.40 A; C/F/I=1-19.
DR PDB; 5OOQ; X-ray; 3.20 A; A/B=81-1073.
DR PDB; 6FSZ; EM; 4.60 A; MM=1-1073.
DR PDB; 6FT6; EM; 3.90 A; MM=80-1073.
DR PDB; 6LQS; EM; 3.80 A; M4=1-1073.
DR PDB; 7AJT; EM; 4.60 A; EN=1-1073.
DR PDB; 7AJU; EM; 3.80 A; EN=1-1073.
DR PDB; 7D4I; EM; 4.00 A; M4=1-1073.
DR PDBsum; 2XGJ; -.
DR PDBsum; 4QU4; -.
DR PDBsum; 4U4C; -.
DR PDBsum; 4WFD; -.
DR PDBsum; 5OOQ; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; P47047; -.
DR SMR; P47047; -.
DR BioGRID; 33705; 317.
DR ComplexPortal; CPX-1678; TRAMP complex variant 4-1.
DR ComplexPortal; CPX-1679; TRAMP complex variant 4-2.
DR ComplexPortal; CPX-1680; TRAMP complex variant 5-1.
DR DIP; DIP-6394N; -.
DR ELM; P47047; -.
DR IntAct; P47047; 20.
DR MINT; P47047; -.
DR STRING; 4932.YJL050W; -.
DR iPTMnet; P47047; -.
DR MaxQB; P47047; -.
DR PaxDb; P47047; -.
DR PRIDE; P47047; -.
DR EnsemblFungi; YJL050W_mRNA; YJL050W; YJL050W.
DR GeneID; 853397; -.
DR KEGG; sce:YJL050W; -.
DR SGD; S000003586; MTR4.
DR VEuPathDB; FungiDB:YJL050W; -.
DR eggNOG; KOG0948; Eukaryota.
DR GeneTree; ENSGT00940000156183; -.
DR HOGENOM; CLU_002902_0_1_1; -.
DR InParanoid; P47047; -.
DR OMA; IMLKNYN; -.
DR BioCyc; YEAST:G3O-31514-MON; -.
DR BRENDA; 3.6.4.13; 984.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR EvolutionaryTrace; P47047; -.
DR PRO; PR:P47047; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47047; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008143; F:poly(A) binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:CACAO.
DR GO; GO:0006397; P:mRNA processing; IMP:SGD.
DR GO; GO:0043629; P:ncRNA polyadenylation; IDA:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IGI:SGD.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0000292; P:RNA fragment catabolic process; IMP:CACAO.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:SGD.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IMP:SGD.
DR DisProt; DP01867; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011254; Prismane-like_sf.
DR InterPro; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; rRNA processing.
FT CHAIN 1..1073
FT /note="ATP-dependent RNA helicase DOB1"
FT /id="PRO_0000102092"
FT DOMAIN 158..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 393..597
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 262..265
FT /note="DEVH box"
FT COMPBIAS 30..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:4WFD"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:2XGJ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2XGJ"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:4U4C"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4QU4"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4QU4"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 465..469
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4QU4"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:4U4C"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 565..572
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 587..595
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:2XGJ"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 609..635
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 642..664
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:4U4C"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 688..700
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 704..708
FT /evidence="ECO:0007829|PDB:5OOQ"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 716..727
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 755..763
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 767..774
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 786..800
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:2XGJ"
FT TURN 810..814
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 819..837
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 839..841
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:2XGJ"
FT HELIX 847..871
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 876..891
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 903..909
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 916..925
FT /evidence="ECO:0007829|PDB:4U4C"
FT TURN 926..930
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 933..944
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 957..979
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 986..992
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 998..1006
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 1010..1015
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 1021..1043
FT /evidence="ECO:0007829|PDB:4U4C"
FT TURN 1044..1046
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 1048..1061
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 1064..1067
FT /evidence="ECO:0007829|PDB:4U4C"
SQ SEQUENCE 1073 AA; 122055 MW; 1FA9EAADC546F669 CRC64;
MDSTDLFDVF EETPVELPTD SNGEKNADTN VGDTPDHTQD KKHGLEEEKE EHEENNSENK
KIKSNKSKTE DKNKKVVVPV LADSFEQEAS REVDASKGLT NSETLQVEQD GKVRLSHQVR
HQVALPPNYD YTPIAEHKRV NEARTYPFTL DPFQDTAISC IDRGESVLVS AHTSAGKTVV
AEYAIAQSLK NKQRVIYTSP IKALSNQKYR ELLAEFGDVG LMTGDITINP DAGCLVMTTE
ILRSMLYRGS EVMREVAWVI FDEVHYMRDK ERGVVWEETI ILLPDKVRYV FLSATIPNAM
EFAEWICKIH SQPCHIVYTN FRPTPLQHYL FPAHGDGIYL VVDEKSTFRE ENFQKAMASI
SNQIGDDPNS TDSRGKKGQT YKGGSAKGDA KGDIYKIVKM IWKKKYNPVI VFSFSKRDCE
ELALKMSKLD FNSDDEKEAL TKIFNNAIAL LPETDRELPQ IKHILPLLRR GIGIHHSGLL
PILKEVIEIL FQEGFLKVLF ATETFSIGLN MPAKTVVFTS VRKWDGQQFR WVSGGEYIQM
SGRAGRRGLD DRGIVIMMID EKMEPQVAKG MVKGQADRLD SAFHLGYNMI LNLMRVEGIS
PEFMLEHSFF QFQNVISVPV MEKKLAELKK DFDGIEVEDE ENVKEYHEIE QAIKGYREDV
RQVVTHPANA LSFLQPGRLV EISVNGKDNY GWGAVVDFAK RINKRNPSAV YTDHESYIVN
VVVNTMYIDS PVNLLKPFNP TLPEGIRPAE EGEKSICAVI PITLDSIKSI GNLRLYMPKD
IRASGQKETV GKSLREVNRR FPDGIPVLDP VKNMKIEDED FLKLMKKIDV LNTKLSSNPL
TNSMRLEELY GKYSRKHDLH EDMKQLKRKI SESQAVIQLD DLRRRKRVLR RLGFCTPNDI
IELKGRVACE ISSGDELLLT ELIFNGNFNE LKPEQAAALL SCFAFQERCK EAPRLKPELA
EPLKAMREIA AKIAKIMKDS KIEVVEKDYV ESFRHELMEV VYEWCRGATF TQICKMTDVY
EGSLIRMFKR LEELVKELVD VANTIGNSSL KEKMEAVLKL IHRDIVSAGS LYL
