ID A0A0L7R1C0_9HYME Unreviewed; 1147 AA.
AC A0A0L7R1C0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:KOC64637.1};
GN ORFNames=WH47_12101 {ECO:0000313|EMBL:KOC64637.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC64637.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC64637.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC64637.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414668; KOC64637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7R1C0; -.
DR STRING; 597456.A0A0L7R1C0; -.
DR Proteomes; UP000053825; 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; 1.10.287.510; Helix hairpin bin; 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; 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 Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 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:UP000053825};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 404..502
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 1083..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 466..535
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 595..706
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 743..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1083..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1147 AA; 133494 MW; DE29227933D1D25F CRC64;
MSRIRRLSIR GIRNFGDDND EALIRFSRPL TLILGPNGTG KTTIIEALKF ATCGEFPPGS
DRGKFFIHDP TLSKTSSVRG VVRAEIIDAT GNLYTICRVI ESTKTNVSMK FKTLDSALSR
VNKDTKECEE RLKAIGGEES TISNILANER VTNGSLRQQI KDQQKKVAFR NKILNETLSA
WNLDTADSNI SEIEVIALSK RLEEKMRELE HKVEENRIKR EQEEKELQKT LGTTTNKLHS
IESKIEEVKI TIQQLNETMD ADAVKKEIID NIKLRNEMEM NLNIVDEEIA SLLKQNSLQS
ELELNKSTLL SKEEEIQKLK SKYEEAIMNL LDIKELSQTK LKSNLDVIQE ELVNEIESIN
RKIQIEEHQL TTLETTISHN ERELQKKRKE IDLDKEKISS ICDYKNFDEA LLLQSKMVKD
LQDKRGMYAH KGAAYKEYMK ELKETNPCCP LCHRSFDERE TVVKLLKEME NEMKNHPNCL
KECEKELKIQ REKYDKMLQL KPIVEKIMHF EQIELEKLKN HLQKSENRLR KSRSIEMELK
QKKLDPENKL TMCKDIIGVI ILWDRYIDEI IELKQIVDNF QTRMIAAGIK TGRSLGEAQT
QRDNLKMSLK NIRDDLEKLQ SRLNTHNEKI HNARQEQNAL HEEQLKIRTG MQKLKELKDR
QEALYSKEIS LGKLVNTLRQ KVTAAESELN SKIDKLERKK KDNREKLEMD IKLLAEGTRR
LSELQKVQDE VDAFVYSKIP EFLECSEMKI KNYEKSLNEL LHQKNDIETT INKLKEEISR
QEVRKRELSD NLTLRKVQET TNSLQQQCLN LKERLNVINY SQVIQERQNL LNQEQTLLRQ
KNIVKGNQEE LEKAVQQYTH ELKREQYRQA RKSYKNKCIE LTVVEEAILN LKAYSRVLDT
AMIEYHEERM ATVNRIMKQM WRLVYTGTDT SSIEIRTDAT QGIGSARRTY NYKLVQTKHG
HEMDMKGRCS AGQKVLASII IRLALAETFC KDCGILALDE PTTNLDQENA DSLANALAKV
VKLRSQHQKN FQLIVISHDE KFVFKLAELS SNKGFYQLYR KNTGYTAIRH CLVENQDHFA
SGDIKEEASS DEEINEYSKS RNKVQSEIGA QGKTYNDQTR QKKRQVSDTD NEDHTENRAS
KKRYVFQ
//
