DNA2_MOUSE
ID DNA2_MOUSE Reviewed; 1062 AA.
AC Q6ZQJ5; Q14BM9; Q8BSZ0; Q8R3J3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease DNA2;
DE AltName: Full=DNA replication ATP-dependent helicase-like homolog;
DE Includes:
DE RecName: Full=DNA replication nuclease DNA2;
DE EC=3.1.-.-;
DE Includes:
DE RecName: Full=DNA replication ATP-dependent helicase DNA2;
DE EC=3.6.4.12;
GN Name=Dna2; Synonyms=Dna2l, Kiaa0083;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 263-1078 (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair in
CC nucleus and mitochondrion. Involved in Okazaki fragments processing by
CC cleaving long flaps that escape FEN1: flaps that are longer than 27
CC nucleotides are coated by replication protein A complex (RPA), leading
CC to recruit DNA2 which cleaves the flap until it is too short to bind
CC RPA and becomes a substrate for FEN1. Also involved in 5'-end resection
CC of DNA during double-strand break (DSB) repair: recruited by BLM and
CC mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is
CC prevented by the presence of RPA. Also involved in DNA replication
CC checkpoint independently of Okazaki fragments processing. Possesses
CC different enzymatic activities, such as single-stranded DNA (ssDNA)-
CC dependent ATPase, 5'-3' helicase and endonuclease activities. While the
CC ATPase and endonuclease activities are well-defined and play a key role
CC in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase
CC activity is subject to debate. According to various reports, the
CC helicase activity is weak and its function remains largely unclear.
CC Helicase activity may promote the motion of DNA2 on the flap, helping
CC the nuclease function (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Interacts with BLM and WDHD1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q6ZQJ5; P70371: Terf1; NbExp=4; IntAct=EBI-6919222, EBI-6919183;
CC Q6ZQJ5; O35144: Terf2; NbExp=4; IntAct=EBI-6919222, EBI-6919263;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZQJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQJ5-2; Sequence=VSP_021872, VSP_021873;
CC -!- PTM: Acetylated by EP300, leading to stimulate the 5'-3' endonuclease,
CC the 5'-3' helicase and DNA-dependent ATPase activities, possibly by
CC increasing DNA substrate affinity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129051; BAC97861.1; ALT_INIT; mRNA.
DR EMBL; AK028381; BAC25919.1; -; mRNA.
DR EMBL; BC025182; AAH25182.1; -; mRNA.
DR EMBL; BC115716; AAI15717.1; -; mRNA.
DR CCDS; CCDS35923.1; -. [Q6ZQJ5-1]
DR RefSeq; NP_796346.2; NM_177372.3. [Q6ZQJ5-1]
DR PDB; 5EAN; X-ray; 2.36 A; A=1-1056.
DR PDB; 5EAW; X-ray; 3.00 A; A/B=1-1056.
DR PDB; 5EAX; X-ray; 3.05 A; A/B=1-1056.
DR PDBsum; 5EAN; -.
DR PDBsum; 5EAW; -.
DR PDBsum; 5EAX; -.
DR AlphaFoldDB; Q6ZQJ5; -.
DR SMR; Q6ZQJ5; -.
DR BioGRID; 236484; 3.
DR IntAct; Q6ZQJ5; 2.
DR MINT; Q6ZQJ5; -.
DR STRING; 10090.ENSMUSP00000115750; -.
DR iPTMnet; Q6ZQJ5; -.
DR PhosphoSitePlus; Q6ZQJ5; -.
DR EPD; Q6ZQJ5; -.
DR MaxQB; Q6ZQJ5; -.
DR PaxDb; Q6ZQJ5; -.
DR PeptideAtlas; Q6ZQJ5; -.
DR PRIDE; Q6ZQJ5; -.
DR ProteomicsDB; 279738; -. [Q6ZQJ5-1]
DR ProteomicsDB; 279739; -. [Q6ZQJ5-2]
DR Antibodypedia; 28503; 153 antibodies from 26 providers.
DR DNASU; 327762; -.
DR Ensembl; ENSMUST00000092462; ENSMUSP00000090119; ENSMUSG00000036875. [Q6ZQJ5-2]
DR Ensembl; ENSMUST00000131422; ENSMUSP00000115750; ENSMUSG00000036875. [Q6ZQJ5-1]
DR GeneID; 327762; -.
DR KEGG; mmu:327762; -.
DR UCSC; uc007fji.2; mouse. [Q6ZQJ5-1]
DR CTD; 1763; -.
DR MGI; MGI:2443732; Dna2.
DR VEuPathDB; HostDB:ENSMUSG00000036875; -.
DR eggNOG; KOG1805; Eukaryota.
DR GeneTree; ENSGT00780000122010; -.
DR HOGENOM; CLU_001666_2_0_1; -.
DR InParanoid; Q6ZQJ5; -.
DR OMA; NYCEAAI; -.
DR OrthoDB; 633768at2759; -.
DR PhylomeDB; Q6ZQJ5; -.
DR TreeFam; TF314903; -.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69166; Removal of the Flap Intermediate.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 327762; 25 hits in 111 CRISPR screens.
DR ChiTaRS; Dna2; mouse.
DR PRO; PR:Q6ZQJ5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6ZQJ5; protein.
DR Bgee; ENSMUSG00000036875; Expressed in fetal liver hematopoietic progenitor cell and 193 other tissues.
DR Genevisible; Q6ZQJ5; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005760; C:gamma DNA polymerase complex; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; ISS:UniProtKB.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO:MGI.
DR GO; GO:0006264; P:mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IMP:BHF-UCL.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:BHF-UCL.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR026851; Dna2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF433; PTHR10887:SF433; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
KW DNA damage; DNA repair; DNA replication; DNA-binding; Endonuclease;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1062
FT /note="DNA replication ATP-dependent helicase/nuclease
FT DNA2"
FT /id="PRO_0000263604"
FT REGION 82..520
FT /note="Nuclease activity"
FT /evidence="ECO:0000250"
FT REGION 521..1062
FT /note="Helicase activity"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 932..966
FT /note="GCSPSDIGVIAPYRQQLRIISDLLARSSVGMVEVN -> AAPQTLASSPRTD
FT SSCGSSATYWPGLLLGWLRLTQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021872"
FT VAR_SEQ 967..1062
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021873"
FT CONFLICT 285
FT /note="I -> K (in Ref. 2; BAC25919)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="P -> L (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="I -> M (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="T -> M (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="A -> V (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="P -> S (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="R -> Q (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT CONFLICT 1037
FT /note="A -> T (in Ref. 3; AAH25182)"
FT /evidence="ECO:0000305"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5EAW"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 59..74
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5EAX"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 204..225
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 252..268
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 273..287
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 290..301
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 349..367
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 436..453
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 475..484
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 532..539
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 541..550
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:5EAW"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 587..596
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 617..625
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 629..640
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 641..649
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 655..668
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 673..679
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 680..692
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 708..710
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 715..721
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 727..734
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 750..753
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 757..762
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 765..767
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 770..773
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 775..779
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 780..787
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 799..803
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 804..807
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 810..814
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 821..824
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 832..841
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 848..851
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 852..856
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 864..871
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 881..887
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 893..897
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 911..913
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 915..930
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 938..941
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 945..957
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 963..966
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 968..971
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 976..982
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:5EAX"
FT HELIX 995..997
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 999..1006
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 1008..1017
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 1019..1022
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 1026..1036
FT /evidence="ECO:0007829|PDB:5EAN"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:5EAN"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:5EAN"
FT HELIX 1050..1053
FT /evidence="ECO:0007829|PDB:5EAN"
SQ SEQUENCE 1062 AA; 119447 MW; CD009CB89ACA775C CRC64;
MEPLDELDLL LLEEDGGAEA VPRVELLRKK ADALFPETVL SRGVDNRYLV LAVETSQNER
GAEEKRLHVT ASQDREHEVL CILRNGWSSV PVEPGDIVHL EGDCTSEPWI IDDDFGYFIL
YPDMMISGTS VASSIRCLRR AVLSETFRGS DPATRQMLIG TILHEVFQKA ISESFAPERL
QELALQTLRE VRHLKEMYRL NLSQDEILCE VEEYLPSFSK WAEDFMRKGP SSEFPQMQLS
LPSDGSNRSS PCNIEVVKSL DIEESIWSPR FGLKGKIDVT VGVKIHRDCK MKYKVMPLEL
KTGKESNSIE HRSQVVLYTL LSQERREDPE AGWLLYLKTG QMYPVPANHL DKRELLKLRN
WLAASLLHRV SRAAPGEEAR LSALPQIIEE EKTCKYCSQI GNCALYSRAV EEQGDDASIP
EAMLSKIQEE TRHLQLAHLK YFSLWCLMLT LESQSKDNRK THQSIWLTPA SELEESGNCV
GNLVRTEPVS RVCDGQYLHN FQRKNGPMPA TNLMAGDRII LSGEERKLFA LSKGYVKKMN
KAAVTCLLDR NLSTLPATTV FRLDREERHG DISTPLGNLS KLMESTDPSK RLRELIIDFR
EPQFIAYLSS VLPHDAKDTV ANILKGLNKP QRQAMKRVLL SKDYTLIVGM PGTGKTTTIC
ALVRILSACG FSVLLTSYTH SAVDNILLKL AKFKVGFLRL GQSHKVHPDI QKFTEEEICR
SRSIASLAHL EELYNSHPIV ATTCMGINHP IFSRKTFDFC IVDEASQISQ PVCLGPLFFS
RRFVLVGDHQ QLPPLVVNRE ARALGMSESL FKRLERNESA VVQLTVQYRM NRKIMSLSNK
LTYAGKLECG SDRVANAVLA LPNLKDARLS LQLYADYSDS PWLAGVLEPD NPVCFLNTDK
VPAPEQVENG GVSNVTEARL IVFLTSTFIK AGCSPSDIGV IAPYRQQLRI ISDLLARSSV
GMVEVNTVDK YQGRDKSLIL VSFVRSNEDG TLGELLKDWR RLNVALTRAK HKLILLGSVS
SLKRFPPLGT LFDHLNAEQL ILDLPSREHE SLSHILGDCQ RD
