ID   A0A3P8P6Q0_ASTCA        Unreviewed;      1074 AA.
AC   A0A3P8P6Q0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=RAD50 homolog, double strand break repair protein {ECO:0000313|Ensembl:ENSACLP00000012686.1};
GN   Name=RAD50 {ECO:0000313|Ensembl:ENSACLP00000012686.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000012686.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000012686.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000012686.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   AlphaFoldDB; A0A3P8P6Q0; -.
DR   STRING; 8154.ENSACLP00000012686; -.
DR   Ensembl; ENSACLT00000012998.1; ENSACLP00000012686.1; ENSACLG00000008504.1.
DR   GeneTree; ENSGT00390000018781; -.
DR   OMA; NIIFCHQ; -.
DR   Proteomes; UP000265100; Chromosome 23.
DR   Bgee; ENSACLG00000008504; Expressed in ovary and 1 other cell type or tissue.
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:0006281; P:DNA 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
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; PF04423; Rad50_zn_hook; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 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   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|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          560..659
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          145..274
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          328..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          637..706
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          766..793
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          835..863
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         606
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         609
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1074 AA;  126116 MW;  C6A04787F637BAD5 CRC64;
     MLQDAQRTVV RAQIELSLSD IKGEEIEIQR FVSCSLIENK YSFKSEEQNI KRTKDGRRVS
     RSVKCGDLHQ EITSALGVSK SVLNDVIFCH QEESNWPLSE DRVLKEKFDS IFNVTKYNKA
     RSKMHELRLK QSRRVEQCQA ELFYLEKNKE KAQHLRDNVA QKQADLRASQ NLILHIENQI
     DPLETLLSDI KMKLENVTKL ENETKALDSL RKQMEEHNKE LEETMEEVFQ GSDEQLQHTY
     DNHQRTVMEK EQKLQQHQEE LQTFDQEYQR LTRETNDLLY TMTLLFIHMS SVSQVHSLSS
     CLEMEGYDQL PFTVSQLESF YHQVTHRLEQ ENERVSQLLV RRAELQKLEQ QKQQSVDEMR
     DRKTYMERTV EMKRDERQKK QQELKNITEE LQRLQDSCSR LQELENKLAE VEREDAVQSS
     SVEELKAEVE ELQEEKAELD CTQRQLDKEM ETLNMHTAAL TQMDILKKGK AEMEEQILQI
     RSRHCEDLVS LLGHFPNKKE LEDWVSSKSK EIGSTRDRLT KLKMDLASNE QNKSHITAEL
     LKKELQLATD EEKFLNVCSS RDLEHDLSNL QRELDEIFKT KALLAGTKVV YTQFISELSE
     HREPCCPVCR RSFPSESEVQ EVVRVLQSKL HLVPEKLKIT EQDLERTERR REEIVALRPV
     RYSVRDFQEN ELPALRKRLQ TVDREAERLK GDVEEQEALL AILRSEEEKA KDCLQGISLM
     DSYLVESKID QQASKLQEVN LDNTFQQLSQ DKHETQDQLD TTYSTIVRKH KQIQDQQEQI
     QRLKSAAIEM RDEQLQLIRD KQKQQHLEEL SAEIAARMEA LTTEIREGNE ELCPLSAALE
     KLQQEKQKLV EQKKQREEEE QKKVDAYIKF TAGRRLIISV GQKPCEGHQS LFLCCFHRAI
     VKFHSMKMDE INQNIRDLWR STYRGQDIEY IEIRSEVEER SERRRSYNYR VVMMRGDADV
     NMRGRCSAGQ KVLASLIIRL ALAEAFCLDC GILALDEPTT NLDRENIESL ADALVEIIRT
     RSQQRHFQLL IITHDEDFVQ LLVRSGCIQH FYRISKNQDQ NSKITKQSTA FLSV
//