SUB2_YEAST
ID SUB2_YEAST Reviewed; 446 AA.
AC Q07478; D6VRR5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=ATP-dependent RNA helicase SUB2;
DE EC=3.6.4.13;
DE AltName: Full=Suppressor of BRR1 protein 2;
GN Name=SUB2; OrderedLocusNames=YDL084W;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [5]
RP FUNCTION.
RX PubMed=11696331; DOI=10.1016/s0960-9822(01)00529-2;
RA Jensen T.H., Boulay J., Rosbash M., Libri D.;
RT "The DECD box putative ATPase Sub2p is an early mRNA export factor.";
RL Curr. Biol. 11:1711-1715(2001).
RN [6]
RP ERRATUM OF PUBMED:11696331.
RA Jensen T.H., Boulay J., Rosbash M., Libri D.;
RL Curr. Biol. 14:447-447(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-112; ASP-174; ASP-215; CYS-217 AND
RP SER-247.
RX PubMed=11156602; DOI=10.1101/gad.851701;
RA Zhang M., Green M.R.;
RT "Identification and characterization of yUAP/Sub2p, a yeast homolog of the
RT essential human pre-mRNA splicing factor hUAP56.";
RL Genes Dev. 15:30-35(2001).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-8; GLN-122; VAL-135; LYS-173 AND LYS-403.
RX PubMed=11156603; DOI=10.1101/gad.852101;
RA Libri D., Graziani N., Saguez C., Boulay J.;
RT "Multiple roles for the yeast SUB2/yUAP56 gene in splicing.";
RL Genes Dev. 15:36-41(2001).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASP-22; GLU-83; LEU-142; ILE-146 AND GLN-308.
RX PubMed=11156604; DOI=10.1101/gad.851301;
RA Kistler A.L., Guthrie C.;
RT "Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement
RT for sub2, an essential spliceosomal ATPase.";
RL Genes Dev. 15:42-49(2001).
RN [10]
RP FUNCTION.
RX PubMed=11463828; DOI=10.1128/mcb.21.16.5459-5470.2001;
RA Fan H.-Y., Merker R.J., Klein H.L.;
RT "High-copy-number expression of Sub2p, a member of the RNA helicase
RT superfamily, suppresses hpr1-mediated genomic instability.";
RL Mol. Cell. Biol. 21:5459-5470(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH YRA1.
RX PubMed=11675790; DOI=10.1038/35098113;
RA Straesser K., Hurt E.;
RT "Splicing factor Sub2p is required for nuclear mRNA export through its
RT interaction with Yra1p.";
RL Nature 413:648-652(2001).
RN [12]
RP FUNCTION.
RX PubMed=12093753; DOI=10.1093/emboj/cdf335;
RA Jimeno S., Rondon A.G., Luna R., Aguilera A.;
RT "The yeast THO complex and mRNA export factors link RNA metabolism with
RT transcription and genome instability.";
RL EMBO J. 21:3526-3535(2002).
RN [13]
RP INTERACTION WITH SAC3.
RX PubMed=12411502; DOI=10.1093/emboj/cdf590;
RA Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M.,
RA Ihrig P., Lechner J., Hurt E.;
RT "The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock
RT at the nucleoplasmic entrance of the nuclear pores.";
RL EMBO J. 21:5843-5852(2002).
RN [14]
RP FUNCTION.
RX PubMed=12034490; DOI=10.1016/s0378-1119(02)00482-1;
RA West R.W. Jr., Milgrom E.;
RT "DEAD-box RNA helicase Sub2 is required for expression of lacZ fusions in
RT Saccharomyces cerevisiae and is a dosage-dependent suppressor of RLR1
RT (THO2).";
RL Gene 288:19-27(2002).
RN [15]
RP FUNCTION, INTERACTION WITH HPR1; YRA1 AND YRA2, AND ASSOCIATION WITH MRNP
RP COMPLEXES.
RX PubMed=12417727; DOI=10.1128/mcb.22.23.8241-8253.2002;
RA Zenklusen D., Vinciguerra P., Wyss J.-C., Stutz F.;
RT "Stable mRNP formation and export require cotranscriptional recruitment of
RT the mRNA export factors Yra1p and Sub2p by Hpr1p.";
RL Mol. Cell. Biol. 22:8241-8253(2002).
RN [16]
RP FUNCTION, IDENTIFICATION IN THE TREX COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [17]
RP FUNCTION.
RX PubMed=12871933; DOI=10.1074/jbc.m305718200;
RA Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A.;
RT "Molecular evidence that the eukaryotic THO/TREX complex is required for
RT efficient transcription elongation.";
RL J. Biol. Chem. 278:39037-39043(2003).
RN [18]
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 [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [21]
RP FUNCTION.
RX PubMed=15942929; DOI=10.1002/yea.1231;
RA Lahue E., Heckathorn J., Meyer Z., Smith J., Wolfe C.;
RT "The Saccharomyces cerevisiae Sub2 protein suppresses heterochromatic
RT silencing at telomeres and subtelomeric genes.";
RL Yeast 22:537-551(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [23]
RP IDENTIFICATION BY 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: ATP-binding RNA helicase component of the TREX complex
CC involved in transcription elongation and required for the export of
CC mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing
CC and spliceosome assembly. May be involved in rDNA and telomeric
CC silencing, and maintenance of genome integrity.
CC {ECO:0000269|PubMed:10077188, ECO:0000269|PubMed:11156602,
CC ECO:0000269|PubMed:11156603, ECO:0000269|PubMed:11156604,
CC ECO:0000269|PubMed:11463828, ECO:0000269|PubMed:11675790,
CC ECO:0000269|PubMed:11696331, ECO:0000269|PubMed:11979277,
CC ECO:0000269|PubMed:12034490, ECO:0000269|PubMed:12093753,
CC ECO:0000269|PubMed:12417727, ECO:0000269|PubMed:12871933,
CC ECO:0000269|PubMed:15942929}.
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 TREX complex composed of at least SUB2, TEX1,
CC YRA1 and the four THO complex components: HPR1, MFT1, THO2 and THP1.
CC Interacts with HPR1, YRA1, and YRA2. SUB2 may mediate the interaction
CC between the THO complex and YRA1. Associates with growing mRNP
CC complexes during transcription. This association requires the presence
CC of HPR1. Interacts also with SAC3. {ECO:0000269|PubMed:11675790,
CC ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:12411502,
CC ECO:0000269|PubMed:12417727}.
CC -!- INTERACTION:
CC Q07478; Q12159: YRA1; NbExp=5; IntAct=EBI-18500, EBI-29516;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: Present with 51700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; Z74132; CAA98650.1; -; Genomic_DNA.
DR EMBL; AY692907; AAT92926.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11775.1; -; Genomic_DNA.
DR PIR; S67620; S67620.
DR RefSeq; NP_010199.1; NM_001180143.1.
DR PDB; 5SUP; X-ray; 2.60 A; A/B/C=61-446.
DR PDB; 5SUQ; X-ray; 6.00 A; A/C=1-446.
DR PDB; 7APX; EM; 3.40 A; F=48-446.
DR PDB; 7AQO; EM; 4.50 A; F/L=51-446.
DR PDB; 7LUV; EM; 3.70 A; M=1-446.
DR PDBsum; 5SUP; -.
DR PDBsum; 5SUQ; -.
DR PDBsum; 7APX; -.
DR PDBsum; 7AQO; -.
DR PDBsum; 7LUV; -.
DR AlphaFoldDB; Q07478; -.
DR SMR; Q07478; -.
DR BioGRID; 31977; 253.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-5343N; -.
DR IntAct; Q07478; 29.
DR MINT; Q07478; -.
DR STRING; 4932.YDL084W; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; Q07478; -.
DR MaxQB; Q07478; -.
DR PaxDb; Q07478; -.
DR PRIDE; Q07478; -.
DR EnsemblFungi; YDL084W_mRNA; YDL084W; YDL084W.
DR GeneID; 851475; -.
DR KEGG; sce:YDL084W; -.
DR SGD; S000002242; SUB2.
DR VEuPathDB; FungiDB:YDL084W; -.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00960000189190; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q07478; -.
DR OMA; IKPICRK; -.
DR BioCyc; YEAST:G3O-29493-MON; -.
DR PRO; PR:Q07478; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07478; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0000346; C:transcription export complex; 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:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; IGI:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..446
FT /note="ATP-dependent RNA helicase SUB2"
FT /id="PRO_0000055082"
FT DOMAIN 93..268
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 280..441
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..90
FT /note="Q motif"
FT MOTIF 215..218
FT /note="DECD box"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 8
FT /note="D->G: No growth at 37 degrees Celsius; when
FT associated with DEL-135."
FT /evidence="ECO:0000269|PubMed:11156603"
FT MUTAGEN 22
FT /note="D->G: In SUB2-1; no growth at 16 and 37 degrees
FT Celsius; when associated with G-83; M-142 and T-146."
FT /evidence="ECO:0000269|PubMed:11156604"
FT MUTAGEN 83
FT /note="E->G: In SUB2-1; no growth at 16 and 37 degrees
FT Celsius; when associated with G-22; M-142 and T-146."
FT /evidence="ECO:0000269|PubMed:11156604"
FT MUTAGEN 112
FT /note="K->N: Lethal."
FT /evidence="ECO:0000269|PubMed:11156602"
FT MUTAGEN 122
FT /note="Q->R: In SUB2-201; no growth at 37 degrees Celsius;
FT when associated with G-173 and F-403."
FT /evidence="ECO:0000269|PubMed:11156603"
FT MUTAGEN 135
FT /note="Missing: No growth at 37 degrees Celsius; when
FT associated with G-8."
FT /evidence="ECO:0000269|PubMed:11156603"
FT MUTAGEN 142
FT /note="L->M: In SUB2-1; no growth at 16 and 37 degrees
FT Celsius; when associated with G-22; G-83 and T-146."
FT /evidence="ECO:0000269|PubMed:11156604"
FT MUTAGEN 146
FT /note="I->T: In SUB2-1; no growth at 16 and 37 degrees
FT Celsius; when associated with G-22; G-83 and M-142."
FT /evidence="ECO:0000269|PubMed:11156604"
FT MUTAGEN 173
FT /note="K->G: In SUB2-201; no growth at 37 degrees Celsius;
FT when associated with R-122 and F-403."
FT /evidence="ECO:0000269|PubMed:11156603"
FT MUTAGEN 174
FT /note="D->G: In SUB2-100; no growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11156602"
FT MUTAGEN 215
FT /note="D->E: Lethal."
FT /evidence="ECO:0000269|PubMed:11156602"
FT MUTAGEN 217
FT /note="C->A: Lethal."
FT /evidence="ECO:0000269|PubMed:11156602"
FT MUTAGEN 247
FT /note="S->L: Lethal."
FT /evidence="ECO:0000269|PubMed:11156602"
FT MUTAGEN 308
FT /note="Q->R: In SUB2-5; no growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11156604"
FT MUTAGEN 403
FT /note="K->F: In SUB2-201; no growth at 37 degrees Celsius;
FT when associated with R-122 and G-173."
FT /evidence="ECO:0000269|PubMed:11156603"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:5SUP"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:5SUP"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:5SUP"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:5SUP"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:5SUP"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:5SUP"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:5SUP"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:5SUP"
SQ SEQUENCE 446 AA; 50309 MW; AB3605A8C38A560C CRC64;
MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG DKKGSYVGIH
STGFKDFLLK PELSRAIIDC GFEHPSEVQQ HTIPQSIHGT DVLCQAKSGL GKTAVFVLST
LQQLDPVPGE VAVVVICNAR ELAYQIRNEY LRFSKYMPDV KTAVFYGGTP ISKDAELLKN
KDTAPHIVVA TPGRLKALVR EKYIDLSHVK NFVIDECDKV LEELDMRRDV QEIFRATPRD
KQVMMFSATL SQEIRPICRR FLQNPLEIFV DDEAKLTLHG LQQYYIKLEE REKNRKLAQL
LDDLEFNQVI IFVKSTTRAN ELTKLLNASN FPAITVHGHM KQEERIARYK AFKDFEKRIC
VSTDVFGRGI DIERINLAIN YDLTNEADQY LHRVGRAGRF GTKGLAISFV SSKEDEEVLA
KIQERFDVKI AEFPEEGIDP STYLNN
