ID   A0A0P7B2L1_9HYPO        Unreviewed;      1307 AA.
AC   A0A0P7B2L1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=DNA repair protein rad50 {ECO:0000313|EMBL:KPM35647.1};
GN   ORFNames=AK830_g10934 {ECO:0000313|EMBL:KPM35647.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM35647.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM35647.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM35647.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-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}.
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:KPM35647.1}.
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DR   EMBL; LKCW01000241; KPM35647.1; -; Genomic_DNA.
DR   STRING; 78410.A0A0P7B2L1; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000050424; 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.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
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:UP000050424};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..233
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          333..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..622
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          493..527
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          642..669
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          744..785
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          836..884
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          977..1074
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        342..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1307 AA;  150210 MW;  FCA4043CAE1F1DC0 CRC64;
     MSRIDKLSIS GIRSFSPSVR EAIQFNTPLT LIVGYNGSGK TTIIECLKYA TTGELPPNSK
     GGAFIHDPKL CGEKEVLAQV KLQFRSINDR QHVATRSVQL TVKKAARSQK TLDCSLVVVN
     NGERTTTSTR QAQLDEMIPE RLGVSPAILD AVIFCHQDES LWPLSEPAAL KKRFDEIFEA
     LKYTKAIDNL KVLRKKQVEQ LGKLQNDEVH NKVNKDRGER AEERMKALQA EIEASRDSCE
     SISAEMEETQ DKIRTIRETA NTHLEIVHNL NNKREQLEYR QDAVKELKTT IDELHEDDTS
     LENDLAHYED RMHHLQDEAD GNKTQYNDLQ RSLGQSRKDQ SLKLAEQGKH QSDKDKYERQ
     LKLRMEVIQE AAETYGFSGF DGDLTDQHVK NFNDRIQKLL SEKKRDLERM QKENSVELDR
     ATSVITELEG RKAARTQDRV SAKQRMSAIE KRTSVLQNES GRIDVDEGAK AILDGQLEDL
     ESRFQTAQKG FEAANWDRQL NDDNDKLHQL ENENDKLGRE LVECTRLASD RAQLDLRKKE
     LADRKRKLDT LTTTWKPKLD KVIGSEWQAE TLDARFQSVL KDVNKVVADA QKRRDQTRQK
     QQKVEFRMKS AKESRDRNTQ EAASCQQRVV DALLTVRDNA IVEDYAEEVA SVEQQVEDLR
     NELSLFDALV DYYNKCKRML ESKKKCLLCE RHFDDSQASS LDRLGKKIEK NLDPKGKVDV
     EKDLKETMAS LEKLRSVRSA YDTYERLNAK LPSLRDECKA AESEYDTLER QVEEQMAIVS
     SEEEKQNDLE DMSKTVMSIA QTVRDITDSE NQVDRIVSQQ VSGGATRSPE EIHELQAGLS
     EQMRSLKTRI SKLTNDRQRM KDQLNALELE KSELRNKISR AGGQLDKKKD LLAQIQALKD
     DQSHQRDIIH RADEELEQIE PSMIEARSAR DEVLRRGRSK EQVIVEARDA VANSVSEVKM
     MDSDIQDYID RGGPSNLASN QRAIAVLEKA IANTEKEITD LTVRTNKLKQ DIDNGDRKKK
     NINDNLNYRK HLRMLEVIRR DISELEERNA DEDYERLQTE ARSQENQYNR LLAERGSVMG
     TMKTKDEELG RLLQEWEMDY KDAKRKYRES HIRVETTKAA IEDLAQCGSA VDKAVMQFHS
     LKMSEINRIA GELWQSTYQG TDIDTILIRS DNESNTGKRS YNYRLCMVKQ DTEMDMRGRC
     SAGQKVLASI IIRLALAESF GVNCGLIALD EPTTNLDRDN IKSLAESLHM IIKTRQAQSN
     FQLIVITHDE EFLRHMRCSD FCDSFFRVRR DERQNSVISR ESITKIF
//