ID   A0A318Z430_9EURO        Unreviewed;      1301 AA.
AC   A0A318Z430;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=BP01DRAFT_359691 {ECO:0000313|EMBL:PYH42075.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH42075.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH42075.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH42075.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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; KZ821255; PYH42075.1; -; Genomic_DNA.
DR   STRING; 1450539.A0A318Z430; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000248349; Unassembled WGS sequence.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 1.20.58.60; -; 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   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   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..233
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          1047..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          204..252
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          305..346
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          393..438
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          470..527
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          587..632
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          698..730
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          837..878
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1047..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1301 AA;  149663 MW;  A4B3CDA7AAC81414 CRC64;
     MSKIDKLSIL GVRSFDNTRS ETIQFHTPLT LIVGYNGSGK TTIIECLKYA TTGDLPPNSK
     GGAFIHDPKL CGEKEVLAQV KLSFKATSGA KMVATRSLQL TVKKTTRQQK TLEGQLLMVK
     DGERTAISSR VAELDQILPQ YLGVSRAVLD SVIFCHQDES LWPMSEPSVL KKKFDEIFEA
     MKYTKAIDNI KALRKKQNEE LGKYKIMEQH AKEDKEKADR VEKRSIKLQD EIEALRAETH
     QLSQEMRRVA ELADRAWKES ESYSQVLGAL EGKRIEAKSI QTTLDNLKRH LVELDDSDEW
     LESNLEQFET KQLQYQQQEE SQKENYMEIK EQIENARHKL GLKQAEYGKF ENDKANFERQ
     VERRQRMTKE IARSHSIRGF DNVVDQADVD EFMRRVRKIL KEQNQVLERV KREAQSELRE
     AQDSLNQIGQ RKSALQESKI AAKRQIAFND RDAATYQAKL NEINVDEGVQ AALETNIEDT
     VSRLDQAKER SRTASWDKEI QNVNSEIRKF EDESSRLNAE LIEATKKAGD LARLDHLKKE
     LREQERGLGT MKSAHGDRLS KYIKSNWSTD SLEQDFQRVL EEESGHVSKA ERERDGVSRE
     LEQVEFKMKE AKKALNQRQK ELKESIHEIR EAIGDEPEEY LEIVKERQIQ LDLARKDAEQ
     YAGIGSYMKD CLGTAKQSKV CRLCQRGFEA ERQLQAFINK LEGLVKKAQR NLEDEDIKHL
     EEDLNAAREA STAYNTWARL KETEIPSLEK EEEQYVLQQD KLLSQLEEHD KIVSERTEKK
     KDVEALSKTV NTIVKYASDI KSIRSQIEEL SSKQEDNTGS RTLEDIQEEI AGIGERSRAL
     KKTLSKLTHE KEQTLAEINN LELQLRDAKS SLDNAKFQLE KKADLVTRLG EYKNLNNEQR
     AAIAKADKDI ESLTPELLKV QAQYDDISQR AEARERELQQ EISQLYDSIH QLEVASEEID
     AYNERGGPTQ LERSERELQT IENEINELES EQATITREIN RISAQLKDSE NTKRQYADNL
     TYRQATRALD KVNAEIEQLA AQNAEVDRSR FKEESERRTR EHNALAAKQA SKMGEMKSKD
     DQLMQLIADY DTDYKDAAGK YKEAHIKVET TRAAVDDLAR YGGALDKAIM KYHGLKMEEI
     NAIVGELWQK TYRGTDVDTI LIRSDNENAK GNRSYNYRVC MVKQGAEMDM RGRCSAGQKV
     LASIIIRLAL AECFGVNCGL IALDEPTTNL DRDNIRSLAE SLHDIIRARQ QQANFQLIVI
     THDEEFLRHM QCGDFSDYYY RVSRNERQKS IIERQSIAEV M
//