ID   A0A158Q793_9BILA        Unreviewed;      1315 AA.
AC   A0A158Q793;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Zinc-hook domain-containing protein {ECO:0000313|WBParaSite:EEL_0000391001-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000391001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000391001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
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   STRING; 1147741.A0A158Q793; -.
DR   WBParaSite; EEL_0000391001-mRNA-1; EEL_0000391001-mRNA-1; EEL_0000391001.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
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:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
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; IPR004584; Rad50_eukaryotes.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   NCBIfam; TIGR00606; rad50; 1.
DR   PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR   PANTHER; PTHR18867; RAD50; 1.
DR   Pfam; PF13476; AAA_23; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          672..769
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          231..278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          471..583
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          609..664
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          733..808
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          884..1096
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         716
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         719
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1315 AA;  152531 MW;  8A8A35FF6D98CA0C CRC64;
     MDEDQLNVGM DHNYVKSLTK MWNDRKNIYE FYEMFYREIE TLERMSLLDT VELQGIRSVG
     VGPQNATVIE FLSPLTIICG SNGAGKTTII EALKYVTTGE LPKGSFQAFI HDMRLADRSR
     VDASVKLKFR DIRGRSCVVT RRIMQSKGAK GKITNKSEES TIAIEKEPGE WKSLSSKVVD
     CRKEILNLLG LPAAILEYVV FCHQEESSWP LDEPKKLKER FDEIFQVTGY VKAIEILRKE
     LKENQQELRV TEGRLPLLIR QQEEKIELHN EYISLKEQIA GNEKEILLKQ TTLKEDTAKK
     NLKVAELDEA EMSKKKHDMM EAEKQVLVNQ IECCSALDYE GGVENLKREI ESIAHSTEFE
     DMERNRKRIN AEIDEINAKI KEYVAKKMEI DKAIVELKST QMMHDKMIVE RDHFLETYCS
     RFNLRNEQAE VLNQLLRLIE KRREDISNFM SGREEKQTNC QKEIDSISGV LAQITAKIEL
     RNQESKRLEE DIAAVRCNLM EAASSSEKLD HLQHEILEQE KELEVMRKNE ELGTNVEDLR
     NKRDGITSKI ELLKKEYCMR ENAEEIENKI KQKHNELVKF EKELCTLKDK HQTALLDIFN
     TKEPDFPLRE RLTIHARKAE QNLSTAEDEF KIHEKEVSRA QFAVSQIGRE VDQLADQISS
     YRRKITKVVT HENEVETRLD EIKTLLRKSQ QDSGRINGCT FLYEQWEEEV SVRKCCPLCE
     QSYSSTEDSD ILKEKIKQKK KDFTKDAEKL IHKVKEYEAM QNELMELVPY VGMLKQSNSE
     KEKLQENLKK AEEKLHDVEV EFAKSKSERD IILQKLTVIR GVQVDASLMD NIWKSSSDAK
     YDIKLLEAEL GAIECTKRSL SDIRVEIKEN EGKFIELINK LDIIQAAASE RNKLVEKLNA
     SKELRTTLCG KVVQLDSIKK ALDVKEKELE ESKHDLQKLE TQKPIIEAEL QMKKKERFVI
     QNETKNKEAE LLCSLRDVED AAREIEAIDK KLQDVVNSSD DLNNYERDLL KIETEIDVSN
     AKMRNLTEQI DCLNSKQERK RRLDDQLRKL ELRERIKSLN ESLKETEWHG MAIPELREEL
     RTLSEQKKRL ATMEKILASS EYAQFKEEFK KEVVKKCVIK RVIEDLANYI RAVDESVVKF
     HAQKMEEINE VLSSLWEQVY HGNDIETIQI KSESAGENEK KKSYNYRVVM HVGGNEIDMP
     GRCSAGQKML ASILIRIAIS DVFCDKCSII ALDEPTANLD VLKNLGDMLA DIISARCANN
     AKMFQLIVIT HDNRFVEHLR QLCRPEWVYS VSKDGAGLSR VKRHRNLEDA TMREE
//