ID D7LEB9_ARALL Unreviewed; 1234 AA.
AC D7LEB9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN ORFNames=ARALYDRAFT_344958 {ECO:0000313|EMBL:EFH55616.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; GL348716; EFH55616.1; -; Genomic_DNA.
DR RefSeq; XP_002879357.1; XM_002879311.1.
DR AlphaFoldDB; D7LEB9; -.
DR STRING; 81972.D7LEB9; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_4001300; fgenesh1_pg.C_scaffold_4001300; fgenesh1_pg.C_scaffold_4001300.
DR Gramene; fgenesh1_pg.C_scaffold_4001300; fgenesh1_pg.C_scaffold_4001300; fgenesh1_pg.C_scaffold_4001300.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 617..716
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 279..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 477..616
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 777..940
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1234 AA; 143606 MW; EA6B7696F3C2C1B7 CRC64;
MSTVDKMLIK GIRSFDPENK NVVTFFRPLT LIVGANGAGK TTIIECLKVS CTGELPPNAR
SGHSFIHDPK VAGETETKAQ IKLRFKTAAG KDVVCIRSFQ LTQKASKMEY KAIESVLQTI
NPHTGEKVCL SYRCADMDRE IPALMGVSKA ILENVIFVHQ DESNWPLQDP STLKKKFDDI
FSATRYTKAL EVIKKLHKDQ AQEIKTFKLK LENLQTLKDA AYKLRESIAQ DQERTESSKV
QMLELETSIQ KVDAEVHNKE MMLKDLRKLQ DQVSRKTAER STLFKEQQRQ YAELPEENED
TIEELKEWKS KFEERIALLE TKIRKMEREM DDTATTIYSL HNAKTNYMLE ISKLQTEAEA
HMLLKNERDS TIQKIFSHHN LGNVPSTPFG TEVVLNLTNR IKSRLGELEM DLLDKKKSNE
TALSTAWDCY MDANDRWKSI EAQKRAKDEI KMGISKRIEE KEIERDSFEF EISTVDVKQT
DEREKQVQIE LERKTKQNSE LGFESKIEQK QHEIYSMEHK IKTLNRERDV MAGDAEDRVK
LSLKKTEQEN LRKKHKKMSI EREYDDLSLK SREAEKEVNM LQMKIQEVNN SLFKHNKDTE
SRKKYIESKL QALKQESVTI DAYPKLLESA KDERDDRKSK YNMANGMRKM FEPFEDLARQ
HHYCPCCERS FTTDEENSFV KKQRVKASTT GEQLKKLAVE SSNADSVFQQ LDKLRAVFEE
YSKLTSEIIP LAEKSLQEHT EELGQKSQAL DDVLGISAQI KADKDSIEAL VHPLENADRT
FQEIVSYQKQ IEDLEYKLDF RGLGVKTMEE IQSELSSLQS SKDKLHGELE KLRDDQIYME
RDISCLQARW HAVREEKAKA ANLLRDVTKA EEDLERLAEE KSQLDLDVKY LAEALGPLSK
EKEQLLSDYN DMKIRRNQEY EELAEKKRNY QQEVEALLKA SSKINEYAYS CFTRYHDLKK
GERLNDIQEK QRLSESQLQS CEARKNELAG ELNRNKDLMR NQDQLRRNIE DNLNYRTTKA
KVEELTPIHL FSMMLRLNRC RGTVSVYESS ISKNRVELKA AQYKDIDKRH FDQLIQLKTT
EMANKDLDRY YNALDKALMR FHTMKMEEIN KIIRELWQQT YRGQDMDYIR IHSDSEGAGT
RSYSYKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDGP NSESLAGALL RIMEDRKGQE
NFQLIVITHD ERFAQMIGQR QHAEKYYRVA KDDM
//
