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Apaf-1 related killer DARK (Apaf-1/CED-4-related caspase activator Dapaf-1L) (Cell death protein HAC-1) (Death-associated APAF1-related killer, isoform B) (FI21208p1)

 Q7KLI1_DROME            Unreviewed;      1440 AA.
Q7KLI1;
03-OCT-2006, integrated into UniProtKB/TrEMBL.
03-OCT-2006, sequence version 1.
05-DEC-2018, entry version 126.
SubName: Full=Apaf-1 related killer DARK {ECO:0000313|EMBL:AAD45988.1};
SubName: Full=Apaf-1/CED-4-related caspase activator Dapaf-1L {ECO:0000313|EMBL:BAA86939.1};
SubName: Full=Cell death protein HAC-1 {ECO:0000313|EMBL:AAF07207.2};
SubName: Full=Death-associated APAF1-related killer, isoform B {ECO:0000313|EMBL:AAF57916.1};
SubName: Full=FI21208p1 {ECO:0000313|EMBL:AHA95701.1};
Name=Dark {ECO:0000313|EMBL:AAF57916.1,
ECO:0000313|FlyBase:FBgn0263864};
Synonyms=anon-53Fa {ECO:0000313|EMBL:AAF57916.1},
Apaf {ECO:0000313|EMBL:AAF57916.1},
APAF-1 {ECO:0000313|EMBL:AAF57916.1},
Apaf-1 {ECO:0000313|EMBL:AAF57916.1},
apaf-1 {ECO:0000313|EMBL:AAF57916.1},
Apaf-I {ECO:0000313|EMBL:AAF57916.1},
APAF1 {ECO:0000313|EMBL:AAF57916.1},
Apaf1 {ECO:0000313|EMBL:AAF57916.1},
apaf1 {ECO:0000313|EMBL:AAF57916.1},
arc {ECO:0000313|EMBL:AAF57916.1}, ARK {ECO:0000313|EMBL:AAF57916.1},
Ark {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|FlyBase:FBgn0263864},
ark {ECO:0000313|EMBL:AAF57916.1},
Ark-RB {ECO:0000313|EMBL:AHA95701.1},
D-Apaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf {ECO:0000313|EMBL:AAF57916.1},
Dapaf-1 {ECO:0000313|EMBL:AAF57916.1},
dAPAF-1 {ECO:0000313|EMBL:AAF57916.1},
dApaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf-1L {ECO:0000313|EMBL:AAF57916.1},
dapaf-1S {ECO:0000313|EMBL:AAF57916.1},
dApaf1 {ECO:0000313|EMBL:AAF57916.1},
DARK {ECO:0000313|EMBL:AAF57916.1},
dArk {ECO:0000313|EMBL:AAF57916.1},
dark {ECO:0000313|EMBL:AAF57916.1},
Dmel\CG6829 {ECO:0000313|EMBL:AAF57916.1},
HAC-1 {ECO:0000313|EMBL:AAF57916.1},
Hac-1 {ECO:0000313|EMBL:AAF57916.1},
hac-1 {ECO:0000313|EMBL:AAF57916.1},
HAC1 {ECO:0000313|EMBL:AAF57916.1},
Hac1 {ECO:0000313|EMBL:AAF07207.2},
hac1 {ECO:0000313|EMBL:AAF57916.1},
l(2)SH0173 {ECO:0000313|EMBL:AAF57916.1},
T1 {ECO:0000313|EMBL:AAF57916.1};
ORFNames=CG6829 {ECO:0000313|EMBL:AAF57916.1,
ECO:0000313|FlyBase:FBgn0263864},
Dmel_CG6829 {ECO:0000313|EMBL:AAF57916.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAD45988.1};
[1] {ECO:0000313|EMBL:AAF07207.2}
NUCLEOTIDE SEQUENCE.
PubMed=10619022; DOI=10.1016/S1097-2765(00)80385-8;
Zhou L., Song Z., Tittel J., Steller H.;
"HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in
developmental and radiation-induced apoptosis.";
Mol. Cell 4:745-755(1999).
[2] {ECO:0000313|EMBL:BAA86939.1}
NUCLEOTIDE SEQUENCE.
PubMed=10619023; DOI=10.1016/S1097-2765(00)80386-X;
Kanuka H., Sawamoto K., Inohara N., Matsuno K., Okano H., Miura M.;
"Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-
1/CED-4-related caspase activator.";
Mol. Cell 4:757-769(1999).
[3] {ECO:0000313|EMBL:AAD45988.1}
NUCLEOTIDE SEQUENCE.
PubMed=10559939; DOI=10.1038/12984;
Rodriguez A., Oliver H., Zou H., Chen P., Wang X., Abrams J.M.;
"Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an
evolutionarily conserved death pathway.";
Nat. Cell Biol. 1:272-279(1999).
[4] {ECO:0000313|EMBL:AAD45988.1}
NUCLEOTIDE SEQUENCE.
Rodriquez A., Oliver H., Chen P., Zou H., Wang X., Abrams J.M.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:AAF07207.2}
NUCLEOTIDE SEQUENCE.
Zhou L., Song Z., Tittel J., Steller H.;
"HAC-1, a Drosophila homolog of APAF-1 and CED-4, functions in
deveopmental and readiation-induced apoptosis.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[7] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[8] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[9] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[10] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[11] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[12] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[13] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[14] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[15] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[16] {ECO:0000213|PDB:4V4L}
STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS) OF 1-583.
PubMed=21220123; DOI=10.1016/j.str.2010.10.009;
Yuan S., Yu X., Topf M., Dorstyn L., Kumar S., Ludtke S.J., Akey C.W.;
"Structure of the Drosophila apoptosome at 6.9a resolution.";
Structure 19:128-140(2011).
[17] {ECO:0000313|EMBL:AHA95701.1}
NUCLEOTIDE SEQUENCE.
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
[18] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109357; DOI=.1534/g3.115.018929;
FlyBase Consortium;
Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B.,
St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K.,
Strelets V., Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: Impact of High-
Throughput Data.";
G3 (Bethesda) 5:1721-1736(2015).
[19] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109356; DOI=.1534/g3.115.018937;
FlyBase Consortium;
Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B.,
St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B.,
Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: The Rule-
Benders.";
G3 (Bethesda) 5:1737-1749(2015).
[20] {ECO:0000213|PDB:3J9K, ECO:0000213|PDB:3J9L}
STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 1-583 IN COMPLEX
WITH ADP.
PubMed=25644603; DOI=10.1101/gad.255877.114;
Pang Y., Bai X.C., Yan C., Hao Q., Chen Z., Wang J.W., Scheres S.H.,
Shi Y.;
"Structure of the apoptosome: mechanistic insights into activation of
an initiator caspase from Drosophila.";
Genes Dev. 29:277-287(2015).
[21] {ECO:0000213|PDB:5JUL}
STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS).
PubMed=27916517; DOI=10.1016/j.str.2016.11.002;
Cheng T.C., Akey I.V., Yuan S., Yu Z., Ludtke S.J., Akey C.W.;
"A Near-Atomic Structure of the Dark Apoptosome Provides Insight into
Assembly and Activation.";
Structure 25:40-52(2017).
[22] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-3404349, EBI-3404349;
Q9XYF4:Dronc; NbExp=3; IntAct=EBI-3404349, EBI-108311;
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EMBL; AF162659; AAD45988.1; -; mRNA.
EMBL; AF196306; AAF07207.2; -; mRNA.
EMBL; AE013599; AAF57916.1; -; Genomic_DNA.
EMBL; BT150397; AHA95701.1; -; mRNA.
EMBL; AB027531; BAA86939.1; -; mRNA.
RefSeq; NP_725637.1; NM_166207.3.
UniGene; Dm.3047; -.
PDB; 3J9K; EM; 4.10 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e=1-583.
PDB; 3J9L; EM; 4.00 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q=1-583.
PDB; 4V4L; EM; 6.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-583.
PDB; 5JUL; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-1440.
IntAct; Q7KLI1; 2.
STRING; 7227.FBpp0086122; -.
EnsemblMetazoa; FBtr0086968; FBpp0086122; FBgn0263864.
GeneID; 36914; -.
KEGG; dme:Dmel_CG6829; -.
UCSC; CG6829-RB; d. melanogaster.
CTD; 36914; -.
FlyBase; FBgn0263864; Dark.
eggNOG; KOG4658; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000157710; -.
KO; K02084; -.
OMA; NLGCKIL; -.
OrthoDB; EOG091G03E3; -.
ChiTaRS; Dark; fly.
GenomeRNAi; 36914; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0263864; Expressed in 22 organ(s), highest expression level in head mesoderm (Drosophila).
GO; GO:0043293; C:apoptosome; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0043531; F:ADP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IDA:FlyBase.
GO; GO:0050700; F:CARD domain binding; ISM:FlyBase.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:FlyBase.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IPI:FlyBase.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IMP:FlyBase.
GO; GO:0006915; P:apoptotic process; TAS:FlyBase.
GO; GO:0021556; P:central nervous system formation; IMP:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
GO; GO:0002921; P:negative regulation of humoral immune response; IMP:FlyBase.
GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:FlyBase.
GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0034352; P:positive regulation of glial cell apoptotic process; IMP:FlyBase.
GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
GO; GO:0051291; P:protein heterooligomerization; IDA:FlyBase.
GO; GO:0051260; P:protein homooligomerization; IDA:FlyBase.
GO; GO:0046668; P:regulation of retinal cell programmed cell death; NAS:FlyBase.
GO; GO:0010332; P:response to gamma radiation; IDA:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:FlyBase.
GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
GO; GO:1901053; P:sarcosine catabolic process; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR002182; NB-ARC.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00931; NB-ARC; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:3J9K, ECO:0000213|PDB:3J9L,
ECO:0000213|PDB:4V4L, ECO:0000213|PDB:5JUL};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Reference proteome {ECO:0000313|Proteomes:UP000000803}.
DOMAIN 135 303 NB-ARC. {ECO:0000259|Pfam:PF00931}.
SEQUENCE 1440 AA; 165619 MW; 74EFEAD06E54FA74 CRC64;
MDFETGEHQY QYKDILSVFE DAFVDNFDCK DVQDMPKSIL SKEEIDHIIM SKDAVSGTLR
LFWTLLSKQE EMVQKFVEEV LRINYKFLMS PIKTEQRQPS MMTRMYIEQR DRLYNDNQVF
AKYNVSRLQP YLKLRQALLE LRPAKNVLID GVLGSGKTWV ALDVCLSYKV QCKMDFKIFW
LNLKNCNSPE TVLEMLQKLL YQIDPNWTSR SDHSSNIKLR IHSIQAELRR LLKSKPYENC
LLVLLNVQNA KAWNAFNLSC KILLTTRFKQ VTDFLSAATT THISLDHHSM TLTPDEVKSL
LLKYLDCRPQ DLPREVLTTN PRRLSIIAES IRDGLATWDN WKHVNCDKLT TIIESSLNVL
EPAEYRKMFD RLSVFPPSAH IPTILLSLIW FDVIKSDVMV VVNKLHKYSL VEKQPKESTI
SIPSIYLELK VKLENEYALH RSIVDHYNIP KTFDSDDLIP PYLDQYFYSH IGHHLKNIEH
PERMTLFRMV FLDFRFLEQK IRHDSTAWNA SGSILNTLQQ LKFYKPYICD NDPKYERLVN
AILDFLPKIE ENLICSKYTD LLRIALMAED EAIFEEAHKQ VQRFDDRVWF TNHGRFHQHR
QIINLGDNEG RHAVYLHNDF CLIALASGQI LLTDVSLEGE DTYLLRDESD SSDILRMAVF
NQQKHLITLH CNGSVKLWSL WPDCPGRRHS GGSKQQLVNS VVKRFIGSYA NLKIVAFYLN
EDAGLPEANI QLHVAFINGD VSILNWDEQD QEFKLSHVPV LKTMQSGIRC FVQVLKRYYV
VCTSNCTLTV WDLTNGSSNT LELHVFNVEN DTPLALDVFD ERSKTATVLL IFKYSVWRLN
FLPGLSVSLQ SEAVQLPEGS FITCGKRSTD GRYLLLGTSE GLIVYDLKIS DPVLRSNVSE
HIECVDIYEL FDPVYKYIVL CGAKGKQVVH VHTLRSVSGS NSHQNREIAW VHSADEISVM
TKACLEPNVY LRSLMDMTRE RTQLLAVDSK ERIHLIKPAI SRISEWSTIT PTHAASNCKI
NAISAFNDEQ IFVGYVDGVI IDVIHDTALP QQFIEEPIDY LKQVSPNILV ASAHSAQKTV
IFQLEKIDPL QPNDQWPLMM DVSTKYASLQ EGQYIILFSD HGVCHLDIAN PSAFVKPKDS
EEYIVGFDLK NSLLFLAYEN NIIDVFRLIF SCNQLRYEQI CEEEIAQKAK ISYLVATDDG
TMLAMGFENG TLELFAVENR KVQLIYSIEE VHEHCIRQLL FSPCKLLLIS CAEQLCFWNV
THMRNNQLER EQKRRRSRRH KQHSVTQEDA VDAAPIAADI DVDVTFVADE FHPVNRGTAE
LWRNKRGNAI RPELLACVKF VGNEARQFFT DAHFSHFYAI DDEGVYYHLQ LLELSRLQPP
PDPVTLDIAN QYEDLKNLRI LDSPLMQDSD SEGADVVGNL VLEKNGGVAR ATPILEEASS


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