ID TDT_MOUSE Reviewed; 530 AA. AC P09838; Q99PD0; Q99PD1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 3. DT 08-JUN-2016, entry version 168. DE RecName: Full=DNA nucleotidylexotransferase; DE EC=2.7.7.31 {ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551}; DE AltName: Full=Terminal addition enzyme; DE AltName: Full=Terminal deoxynucleotidyltransferase {ECO:0000303|PubMed:3755527}; DE Short=TDT; DE Short=Terminal transferase; GN Name=Dntt; Synonyms=Tdt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3755527; DOI=10.1093/nar/14.14.5777; RA Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.; RT "Isolation and characterization of bovine and mouse terminal RT deoxynucleotidyltransferase cDNAs expressible in mammalian cells."; RL Nucleic Acids Res. 14:5777-5792(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; TISSUE=Thymus; RX PubMed=8464703; DOI=10.1093/nar/21.5.1187; RA Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.; RT "Differential splicing in mouse thymus generates two forms of terminal RT deoxynucleotidyl transferase."; RL Nucleic Acids Res. 21:1187-1191(1993). RN [3] RP SEQUENCE REVISION TO 443-445. RA Doyen N.; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), AND RP CHARACTERIZATION. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=11136823; DOI=10.1084/jem.193.1.89; RA Benedict C.L., Gilfillan S., Kearney J.F.; RT "The long isoform of terminal deoxynucleotidyl transferase (TdtL) RT enters the nucleus and, rather than catalyzing N addition, modulates RT the catalytic activity of the short isoform."; RL J. Exp. Med. 193:89-99(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP PROTEIN SEQUENCE OF 388-393, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS. RX PubMed=7556063; RA Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., RA Rougeon F., Doyen N.; RT "The two isoforms of mouse terminal deoxynucleotidyl transferase RT differ in both the ability to add N regions and subcellular RT localization."; RL EMBO J. 14:4221-4229(1995). RN [8] RP CHARACTERIZATION OF ALTERNATIVE FORMS. RX PubMed=10878023; DOI=10.1074/jbc.M005544200; RA Boule J.-B., Rougeon F., Papanicolaou C.; RT "Comparison of the two murine terminal deoxynucleotidyltransferase RT isoforms. A 20-amino acid insertion in the highly conserved carboxyl- RT terminal region modifies the thermosensitivity but not the catalytic RT activity."; RL J. Biol. Chem. 275:28984-28988(2000). RN [9] RP ERRATUM. RX PubMed=11032847; RA Boule J.-B., Rougeon F., Papanicolaou C.; RL J. Biol. Chem. 275:33184-33184(2000). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S) IN RP COMPLEXES WITH MAGNESIUM; COBALT AND ATP ANALOG. RX PubMed=11823435; DOI=10.1093/emboj/21.3.427; RA Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., RA Sukumar N., Rougeon F., Papanicolaou C.; RT "Crystal structures of a template-independent DNA polymerase: murine RT terminal deoxynucleotidyltransferase."; RL EMBO J. 21:427-439(2002). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 132-530 IN COMPLEXES WITH RP SYNTHETIC INHIBITORS AND NUCLEOTIDE, AND CATALYTIC ACTIVITY. RX PubMed=23968551; DOI=10.1021/jm4010187; RA Costi R., Crucitti G.C., Pescatori L., Messore A., Scipione L., RA Tortorella S., Amoroso A., Crespan E., Campiglia P., Maresca B., RA Porta A., Granata I., Novellino E., Gouge J., Delarue M., Maga G., RA Di Santo R.; RT "New nucleotide-competitive non-nucleoside inhibitors of terminal RT deoxynucleotidyl transferase: discovery, characterization, and crystal RT structure in complex with the target."; RL J. Med. Chem. 56:7431-7441(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 132-530 IN COMPLEXES WITH RP ATP; CTP; TTP; NUCLEOTIDE; MAGNESIUM; MANGANESE AND ZINC, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-342; LEU-398; RP ASP-399; HIS-400; LYS-403; ASP-473 AND HIS-475. RX PubMed=23856622; DOI=10.1016/j.jmb.2013.07.009; RA Gouge J., Rosario S., Romain F., Beguin P., Delarue M.; RT "Structures of intermediates along the catalytic cycle of terminal RT deoxynucleotidyltransferase: dynamical aspects of the two-metal ion RT mechanism."; RL J. Mol. Biol. 425:4334-4352(2013). CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end CC of a DNA initiator (PubMed:23856622). One of the in vivo functions CC of this enzyme is the addition of nucleotides at the junction (N CC region) of rearranged Ig heavy chain and T-cell receptor gene CC segments during the maturation of B- and T-cells. CC {ECO:0000269|PubMed:23856622, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000269|PubMed:23856622, CC ECO:0000269|PubMed:23968551}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:23856622}; CC Note=Can also utilize other divalent cations, such as Mn(2+) and CC Co(2+) (in vitro). {ECO:0000269|PubMed:23856622, ECO:0000305}; CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex CC with DNTTIP2 and core histone. Released from this complex by PCNA. CC Interacts with TRERF1. {ECO:0000250|UniProtKB:P04053}. CC -!- SUBCELLULAR LOCATION: Isoform TDT-S: Nucleus. CC -!- SUBCELLULAR LOCATION: Isoform TDT-L: Cytoplasm. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04053}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=TDT-L; Synonyms=TDT-Large, TdtL; CC IsoId=P09838-1; Sequence=Displayed; CC Note=Inactivated at physiological temperature but is stable at CC lower temperatures.; CC Name=TDT-S; Synonyms=TDT-Small, TdtS; CC IsoId=P09838-2; Sequence=VSP_001309; CC Note=Major form.; CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|PROSITE- CC ProRule:PRU00033}. 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; X04123; CAA27735.1; -; mRNA. DR EMBL; X68670; CAA48634.2; -; mRNA. DR EMBL; AF316014; AAK07884.1; -; mRNA. DR EMBL; AF316015; AAK07885.1; -; mRNA. DR EMBL; AK087978; BAC40071.1; -; mRNA. DR EMBL; AK088709; BAC40518.1; -; mRNA. DR CCDS; CCDS29807.1; -. [P09838-1] DR CCDS; CCDS37984.1; -. [P09838-2] DR PIR; B23595; B23595. DR RefSeq; NP_001036693.1; NM_001043228.1. [P09838-2] DR RefSeq; NP_033371.2; NM_009345.2. [P09838-1] DR UniGene; Mm.25620; -. DR PDB; 1JMS; X-ray; 2.36 A; A=130-530. DR PDB; 1KDH; X-ray; 3.00 A; A=148-530. DR PDB; 1KEJ; X-ray; 3.00 A; A=148-530. DR PDB; 4I27; X-ray; 2.60 A; A=132-530. DR PDB; 4I28; X-ray; 2.15 A; A=132-530. DR PDB; 4I29; X-ray; 2.20 A; A=132-530. DR PDB; 4I2A; X-ray; 1.90 A; A=132-530. DR PDB; 4I2B; X-ray; 2.20 A; A=132-530. DR PDB; 4I2C; X-ray; 2.10 A; A=132-530. DR PDB; 4I2D; X-ray; 2.30 A; A=132-530. DR PDB; 4I2E; X-ray; 2.00 A; A=132-530. DR PDB; 4I2F; X-ray; 2.10 A; A=132-530. DR PDB; 4I2G; X-ray; 2.50 A; A=132-530. DR PDB; 4I2H; X-ray; 2.75 A; A=132-530. DR PDB; 4I2I; X-ray; 2.50 A; A=132-530. DR PDB; 4I2J; X-ray; 2.70 A; A=132-530. DR PDB; 4IQT; X-ray; 2.60 A; A=132-530. DR PDB; 4IQU; X-ray; 2.40 A; A=132-530. DR PDB; 4IQV; X-ray; 2.90 A; A=132-530. DR PDB; 4IQW; X-ray; 2.60 A; A=132-530. DR PDB; 4QZ8; X-ray; 2.70 A; A=132-530. DR PDB; 4QZ9; X-ray; 2.05 A; A=132-530. DR PDB; 4QZA; X-ray; 2.15 A; A=132-530. DR PDB; 4QZB; X-ray; 2.15 A; A=132-530. DR PDB; 4QZC; X-ray; 2.75 A; A=132-530. DR PDB; 4QZD; X-ray; 2.70 A; A=132-530. DR PDB; 4QZE; X-ray; 2.25 A; A=132-530. DR PDB; 4QZF; X-ray; 2.60 A; A=132-530. DR PDB; 4QZG; X-ray; 2.75 A; A=132-530. DR PDB; 4QZH; X-ray; 2.60 A; A=132-530. DR PDB; 4QZI; X-ray; 2.65 A; A=132-530. DR PDBsum; 1JMS; -. DR PDBsum; 1KDH; -. DR PDBsum; 1KEJ; -. DR PDBsum; 4I27; -. DR PDBsum; 4I28; -. DR PDBsum; 4I29; -. DR PDBsum; 4I2A; -. DR PDBsum; 4I2B; -. DR PDBsum; 4I2C; -. DR PDBsum; 4I2D; -. DR PDBsum; 4I2E; -. DR PDBsum; 4I2F; -. DR PDBsum; 4I2G; -. DR PDBsum; 4I2H; -. DR PDBsum; 4I2I; -. DR PDBsum; 4I2J; -. DR PDBsum; 4IQT; -. DR PDBsum; 4IQU; -. DR PDBsum; 4IQV; -. DR PDBsum; 4IQW; -. DR PDBsum; 4QZ8; -. DR PDBsum; 4QZ9; -. DR PDBsum; 4QZA; -. DR PDBsum; 4QZB; -. DR PDBsum; 4QZC; -. DR PDBsum; 4QZD; -. DR PDBsum; 4QZE; -. DR PDBsum; 4QZF; -. DR PDBsum; 4QZG; -. DR PDBsum; 4QZH; -. DR PDBsum; 4QZI; -. DR ProteinModelPortal; P09838; -. DR SMR; P09838; 23-125, 149-530. DR STRING; 10090.ENSMUSP00000062078; -. DR iPTMnet; P09838; -. DR PhosphoSite; P09838; -. DR MaxQB; P09838; -. DR PaxDb; P09838; -. DR PRIDE; P09838; -. DR DNASU; 21673; -. DR Ensembl; ENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1] DR Ensembl; ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2] DR GeneID; 21673; -. DR KEGG; mmu:21673; -. DR UCSC; uc008hlo.1; mouse. [P09838-1] DR CTD; 1791; -. DR MGI; MGI:98659; Dntt. DR eggNOG; KOG2534; Eukaryota. DR eggNOG; COG1796; LUCA. DR GeneTree; ENSGT00530000063002; -. DR HOGENOM; HOG000263600; -. DR HOVERGEN; HBG003670; -. DR InParanoid; P09838; -. DR KO; K00977; -. DR OMA; KTWKAIR; -. DR OrthoDB; EOG7BS4BH; -. DR PhylomeDB; P09838; -. DR TreeFam; TF103012; -. DR BRENDA; 2.7.7.31; 3474. DR EvolutionaryTrace; P09838; -. DR PRO; PR:P09838; -. DR Proteomes; UP000000589; Chromosome 19. DR Bgee; P09838; -. DR CleanEx; MM_DNTT; -. DR ExpressionAtlas; P09838; baseline and differential. DR Genevisible; P09838; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IDA:MGI. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006259; P:DNA metabolic process; IDA:MGI. DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.110; -; 1. DR Gene3D; 3.30.210.10; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR002054; DNA-dir_DNA_pol_X. DR InterPro; IPR019843; DNA_pol-X_BS. DR InterPro; IPR010996; DNA_pol_b-like_N. DR InterPro; IPR028207; DNA_pol_B_palm_palm. DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain. DR InterPro; IPR022312; DNA_pol_X. DR InterPro; IPR027421; DNA_pol_X_lyase_dom. DR InterPro; IPR029398; PolB_thumb. DR InterPro; IPR027292; TdT. DR InterPro; IPR001726; TdT/Mu. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF14792; DNA_pol_B_palm; 1. DR Pfam; PF14791; DNA_pol_B_thumb; 1. DR Pfam; PF10391; DNA_pol_lambd_f; 1. DR Pfam; PF14716; HHH_8; 1. DR PIRSF; PIRSF000817; DNA_NT; 1. DR PIRSF; PIRSF501175; TDT; 1. DR PRINTS; PR00869; DNAPOLX. DR PRINTS; PR00871; DNAPOLXTDT. DR SMART; SM00292; BRCT; 1. DR SMART; SM00483; POLXc; 1. DR SUPFAM; SSF47802; SSF47802; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Terminal addition; Transferase. FT CHAIN 1 530 DNA nucleotidylexotransferase. FT /FTId=PRO_0000218792. FT DOMAIN 27 124 BRCT. {ECO:0000255|PROSITE- FT ProRule:PRU00033}. FT REGION 151 530 Mediates interaction with DNTTIP2. FT {ECO:0000250|UniProtKB:P04053}. FT REGION 258 262 Involved in DNA binding. FT {ECO:0000269|PubMed:11823435, FT ECO:0000269|PubMed:23856622}. FT REGION 333 338 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT REGION 342 345 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT REGION 449 450 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT METAL 343 343 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT METAL 345 345 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT METAL 434 434 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT MOD_RES 134 134 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 483 502 Missing (in isoform TDT-S). FT {ECO:0000303|PubMed:11136823}. FT /FTId=VSP_001309. FT MUTAGEN 342 342 H->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 398 398 L->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 399 399 D->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 400 400 H->A: Reduces enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 403 403 K->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 473 473 D->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 475 475 H->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT CONFLICT 26 26 T -> M (in Ref. 2; CAA48634). FT {ECO:0000305}. FT CONFLICT 99 99 L -> F (in Ref. 2; CAA48634). FT {ECO:0000305}. FT CONFLICT 193 193 R -> G (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 287 287 Q -> K (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 309 309 E -> Q (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 367 367 D -> H (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 441 445 DRRAF -> ECAC (in Ref. 1; CAA27735). FT {ECO:0000305}. FT HELIX 154 156 {ECO:0000244|PDB:4I2A}. FT HELIX 166 181 {ECO:0000244|PDB:4I2A}. FT HELIX 185 199 {ECO:0000244|PDB:4I2A}. FT HELIX 208 211 {ECO:0000244|PDB:4I2A}. FT HELIX 219 231 {ECO:0000244|PDB:4I2A}. FT HELIX 235 242 {ECO:0000244|PDB:4I2A}. FT HELIX 244 253 {ECO:0000244|PDB:4I2A}. FT HELIX 260 268 {ECO:0000244|PDB:4I2A}. FT HELIX 274 279 {ECO:0000244|PDB:4I2A}. FT HELIX 287 294 {ECO:0000244|PDB:4I2A}. FT HELIX 296 300 {ECO:0000244|PDB:4I2A}. FT HELIX 305 322 {ECO:0000244|PDB:4I2A}. FT STRAND 327 330 {ECO:0000244|PDB:4I2A}. FT HELIX 332 335 {ECO:0000244|PDB:4I2A}. FT STRAND 339 342 {ECO:0000244|PDB:4I2A}. FT STRAND 344 349 {ECO:0000244|PDB:4I2A}. FT HELIX 355 372 {ECO:0000244|PDB:4I2A}. FT STRAND 375 381 {ECO:0000244|PDB:4I2A}. FT STRAND 394 396 {ECO:0000244|PDB:4I2A}. FT STRAND 401 411 {ECO:0000244|PDB:4I2A}. FT HELIX 412 414 {ECO:0000244|PDB:4I2A}. FT STRAND 425 437 {ECO:0000244|PDB:4I2A}. FT HELIX 440 442 {ECO:0000244|PDB:4I2A}. FT HELIX 443 451 {ECO:0000244|PDB:4I2A}. FT HELIX 454 468 {ECO:0000244|PDB:4I2A}. FT STRAND 470 472 {ECO:0000244|PDB:4I2A}. FT STRAND 477 479 {ECO:0000244|PDB:4I2A}. FT TURN 480 482 {ECO:0000244|PDB:4I2A}. FT STRAND 504 506 {ECO:0000244|PDB:4I2E}. FT HELIX 511 518 {ECO:0000244|PDB:4I2A}. FT HELIX 525 527 {ECO:0000244|PDB:4I2A}. SQ SEQUENCE 530 AA; 60331 MW; E6B109DCF39C8107 CRC64; MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW TGSRQFERDL RRYATHERKM MLDNHALYDR TKGKTVTISP LDGKVSKLQK ALRVFLEAES EEEIFAHLGL DYIEPWERNA //