SSD1_YEAST
ID SSD1_YEAST Reviewed; 1250 AA.
AC P24276; D6VSS2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein SSD1;
DE AltName: Full=Protein SRK1;
GN Name=SSD1; Synonyms=CLA1, RLD1, SRK1; OrderedLocusNames=YDR293C;
GN ORFNames=D9819.4;
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=1848673; DOI=10.1128/mcb.11.4.2133-2148.1991;
RA Sutton A., Immanuel D., Arndt K.T.;
RT "The SIT4 protein phosphatase functions in late G1 for progression into S
RT phase.";
RL Mol. Cell. Biol. 11:2133-2148(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1645449; DOI=10.1128/mcb.11.6.3369-3373.1991;
RA Wilson R.B., Brenner A.A., White T.B., Engler M.J., Gaughran J.P.,
RA Tatchell K.;
RT "The Saccharomyces cerevisiae SRK1 gene, a suppressor of bcy1 and ins1, may
RT be involved in protein phosphatase function.";
RL Mol. Cell. Biol. 11:3369-3373(1991).
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-492, AND
RP IDENTIFICATION BY 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-491 AND TYR-688, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-164; THR-227;
RP SER-286; SER-322; SER-492 AND TYR-688, AND IDENTIFICATION BY MASS
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Can suppress the lethality due to deletion of SIT4, and
CC partially the defects due to BCY1 disruption. Is implicated in the
CC control of the cell cycle G1 phase.
CC -!- INTERACTION:
CC P24276; P53894: CBK1; NbExp=3; IntAct=EBI-18153, EBI-4110;
CC P24276; P38074: HMT1; NbExp=2; IntAct=EBI-18153, EBI-8394;
CC -!- MISCELLANEOUS: Several alleles of SSD1 exist in different yeast
CC strains.
CC -!- MISCELLANEOUS: Present with 1100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; M60318; AAA35047.1; -; Genomic_DNA.
DR EMBL; M63004; AAA35089.1; -; Genomic_DNA.
DR EMBL; U51031; AAB64469.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12132.1; -; Genomic_DNA.
DR PIR; A39578; A39578.
DR RefSeq; NP_010579.1; NM_001180601.1.
DR PDB; 5NCL; X-ray; 3.15 A; D=205-214.
DR PDB; 7AM1; X-ray; 1.90 A; A/B=339-1250.
DR PDBsum; 5NCL; -.
DR PDBsum; 7AM1; -.
DR AlphaFoldDB; P24276; -.
DR SMR; P24276; -.
DR BioGRID; 32345; 981.
DR DIP; DIP-6449N; -.
DR ELM; P24276; -.
DR IntAct; P24276; 32.
DR MINT; P24276; -.
DR STRING; 4932.YDR293C; -.
DR iPTMnet; P24276; -.
DR MaxQB; P24276; -.
DR PaxDb; P24276; -.
DR PRIDE; P24276; -.
DR EnsemblFungi; YDR293C_mRNA; YDR293C; YDR293C.
DR GeneID; 851887; -.
DR KEGG; sce:YDR293C; -.
DR SGD; S000002701; SSD1.
DR VEuPathDB; FungiDB:YDR293C; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_0_3_1; -.
DR InParanoid; P24276; -.
DR OMA; SLCKVQD; -.
DR BioCyc; YEAST:G3O-29856-MON; -.
DR PRO; PR:P24276; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P24276; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:SGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IGI:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008298; P:intracellular mRNA localization; IDA:SGD.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IGI:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Mitosis;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1250
FT /note="Protein SSD1"
FT /id="PRO_0000166424"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 688
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 540..548
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 581..588
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 615..623
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 632..641
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 645..655
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 683..688
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 701..704
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 712..718
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 720..731
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 742..750
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 766..772
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 780..790
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 791..793
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 796..806
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 809..813
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 814..822
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 829..844
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 857..863
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 878..902
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 903..905
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 907..911
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 916..929
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 938..946
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 951..963
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 969..972
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 973..975
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 984..987
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 997..999
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1002..1015
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1023..1059
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 1060..1063
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1064..1075
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1077..1083
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 1085..1087
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1090..1094
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1095..1097
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1100..1106
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 1107..1110
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1111..1116
FT /evidence="ECO:0007829|PDB:7AM1"
FT TURN 1122..1124
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1128..1130
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1136..1139
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1148..1161
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1168..1176
FT /evidence="ECO:0007829|PDB:7AM1"
FT HELIX 1196..1201
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1206..1209
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1212..1218
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1222..1230
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1232..1235
FT /evidence="ECO:0007829|PDB:7AM1"
FT STRAND 1237..1242
FT /evidence="ECO:0007829|PDB:7AM1"
SQ SEQUENCE 1250 AA; 139954 MW; 3D50FD6838ECA514 CRC64;
MSKNSNVNNN RSQEPNNMFV QTTGGGKNAP KQIHVAHRRS QSELTNLMIE QFTLQKQLEQ
VQAQQQQLMA QQQQLAQQTG QYLSGNSGSN NHFTPQPPHP HYNSNGNSPG MSAGGSRSRT
HSRNNSGYYH NSYDNNNNSN NPGSNSHRKT SSQSSIYGHS RRHSLGLNEA KKAAAEEQAK
RISGGEAGVT VKIDSVQADS GSNSTTEQSD FKFPPPPNAH QGHRRATSNL SPPSFKFPPN
SHGDNDDEFI ATSSTHRRSK TRNNEYSPGI NSNWRNQSQQ PQQQLSPFRH RGSNSRDYNS
FNTLEPPAIF QQGHKHRASN SSVHSFSSQG NNNGGGRKSL FAPYLPQANI PELIQEGRLV
AGILRVNKKN RSDAWVSTDG ALDADIYICG SKDRNRALEG DLVAVELLVV DDVWESKKEK
EEKKRRKDAS MQHDLIPLNS SDDYHNDASV TAATSNNFLS SPSSSDSLSK DDLSVRRKRS
STINNDSDSL SSPTKSGVRR RSSLKQRPTQ KKNDDVEVEG QSLLLVEEEE INDKYKPLYA
GHVVAVLDRI PGQLFSGTLG LLRPSQQANS DNNKPPQSPK IAWFKPTDKK VPLIAIPTEL
APKDFVENAD KYSEKLFVAS IKRWPITSLH PFGILVSELG DIHDPDTEID SILRDNNFLS
NEYLDQKNPQ KEKPSFQPLP LTAESLEYRR NFTDTNEYNI FAISELGWVS EFALHVRNNG
NGTLELGCHV VDVTSHIEEG SSVDRRARKR SSAVFMPQKL VNLLPQSFND ELSLAPGKES
ATLSVVYTLD SSTLRIKSTW VGESTISPSN ILSLEQLDEK LSTGSPTSYL STVQEIARSF
YARRINDPEA TLLPTLSLLE SLDDEKVKVD LNILDRTLGF VVINEIKRKV NSTVAEKIYT
KLGDLALLRR QMQPIATKMA SFRKKIQNFG YNFDTNTADE LIKGVLKIKD DDVRVGIEIL
LFKTMPRARY FIAGKVDPDQ YGHYALNLPI YTHFTAPMRR YADHVVHRQL KAVIHDTPYT
EDMEALKITS EYCNFKKDCA YQAQEQAIHL LLCKTINDMG NTTGQLLTMA TVLQVYESSF
DVFIPEFGIE KRVHGDQLPL IKAEFDGTNR VLELHWQPGV DSATFIPADE KNPKSYRNSI
KNKFRSTAAE IANIELDKEA ESEPLISDPL SKELSDLHLT VPNLRLPSAS DNKQNALEKF
ISTTETRIEN DNYIQEIHEL QKIPILLRAE VGMALPCLTV RALNPFMKRV
