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
//