ID A0A162JF09_9HYPO Unreviewed; 1307 AA.
AC A0A162JF09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Recombination/repair protein Rad50 {ECO:0000313|EMBL:OAA41163.1};
GN ORFNames=BBO_05699 {ECO:0000313|EMBL:OAA41163.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41163.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41163.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41163.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA41163.1}.
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DR EMBL; AZHA01000017; OAA41163.1; -; Genomic_DNA.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000076863; 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..240
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..318
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 389..420
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 580..662
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 701..785
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 843..919
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 977..1106
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 806..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 149806 MW; D39BE9A5DA3C4E11 CRC64;
MSRIEKLSIS GVRSFSPACR EAIQFNTPLT LIVGYNGSGK TTIIECLKYA TTGELPPNSK
GGAFIHDPKL CGEKEVMAQV KLQFRSINDR QHVATRSLQL TVKKTTRSQK TLDCSLVVVN
NGERTTTSTR QAQLDEMIPE RLGVSPAILD AVIFCHQDES LWPLSEPSAL KKRFDEIFEA
LKYTKAIENL KVLRKKQVEE LGKLQNDEAH NKVNKDRGER AEKRMTALQA EIEAAREKCE
AITAEMQDTQ DKIRQKREQA NSFLQVVQNL SNKREQLEYR QDAVNELRQR INELPEDDAS
LERQLAQYEE SMRRQSEEAN RNKIHYSELQ EDLAKSRKSL STKLAEQGKH QSDKEKHERQ
LKMRMEMVQE AAQRHAFRGY DDDLTDVLIK QFNEKIQKLL AEKKRDLERL QKENAAELDK
ASATISELEG QKAARTQDRL SAKQRMGAIE KRTTVLQNES SLIIVDEGLK AVLDGQLGEL
EGKFSQVQQE FETAAWDKHL TEENTKLWQL ESESDKLGRE LIECTRLASE RAQLDFRKKE
LSDRKLKLAT LTETWTPKLD KLIGGGWNPE NIEGKFQALL AAQNKSLQEA RQQQEQTRQK
QAKVDYKLKT VKETYEQKQT QQNECKEQVL AALQSVRESA VIEDYPEEVS ATEQQIETLR
DDLSLIDALK DYYTKCKRAL DAKKTCLLCD RHFDDSQTAS IDRLRAKIDR HLNSKTKVEA
EQDLSEASST LQSLVAVRSQ YDTYERLGKE LPELRNQRKS IETDYESIER LLEEHDAAVT
AEEEKQRDMD DMSKTVSNIG QTLREIQDSE SQVERIASQQ QSAGSGRSAD EIHELQGTVS
EQMRASKNRV AKLTNDRQRA RDQISALELE KSELRNKISL TSGQLDKKED LQGQIHNLKE
ELAHQREAMQ RADQELEKVE PRITEARSIR DDTLKRGRAK EQTITENRDS VAASINEIKM
IESDIQDYED GGGASNLASN QRAIATLEQT ITTTEAEITE LTQRTNKLKQ DIDNGDRTKE
NINDNLNYRK HLRTLEVLRD EIDELEDRNA HEDYERLQGE ARTLENQSNR LFAERGSVMG
AMKTKDEDLD RLLKEWEMDY KDAKQKYRES HIRVETTKAA IEDLAQCGSA VDKAVMQFHA
MKMAEVNRIA GELWQSTYQG TDIDTILIRS DNEGTTGRRN YNYRLCMVKQ DAEMDMRGRC
SAGQKVLASI IVRLALAESF GVNCGLVALD EPTTNLDRDN IKSLAESLHA IIRARQAQSN
FQLIVITHDE DFLRHMRCSD FCDSFFRVKR DEKQNSVISR ESITKIF
//
